Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Vaccines, Synthetic: Small synthetic peptides that mimic surface antigens of pathogens and are immunogenic, or vaccines manufactured with the aid of recombinant DNA techniques. The latter vaccines may also be whole viruses whose nucleic acids have been modified.Immunotoxins: Semisynthetic conjugates of various toxic molecules, including RADIOACTIVE ISOTOPES and bacterial or plant toxins, with specific immune substances such as IMMUNOGLOBULINS; MONOCLONAL ANTIBODIES; and ANTIGENS. The antitumor or antiviral immune substance carries the toxin to the tumor or infected cell where the toxin exerts its poisonous effect.Membrane Fusion: The adherence and merging of cell membranes, intracellular membranes, or artificial membranes to each other or to viruses, parasites, or interstitial particles through a variety of chemical and physical processes.Epitopes: Sites on an antigen that interact with specific antibodies.Viral Fusion Proteins: Proteins, usually glycoproteins, found in the viral envelopes of a variety of viruses. They promote cell membrane fusion and thereby may function in the uptake of the virus by cells.Cell Fusion: Fusion of somatic cells in vitro or in vivo, which results in somatic cell hybridization.Genetic Vectors: DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Immunoconjugates: Combinations of diagnostic or therapeutic substances linked with specific immune substances such as IMMUNOGLOBULINS; MONOCLONAL ANTIBODIES; or ANTIGENS. Often the diagnostic or therapeutic substance is a radionuclide. These conjugates are useful tools for specific targeting of DRUGS and RADIOISOTOPES in the CHEMOTHERAPY and RADIOIMMUNOTHERAPY of certain cancers.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Glutathione Transferase: A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Enzyme-Linked Immunosorbent Assay: An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Mice, Inbred BALB CBlotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Bacterial Proteins: Proteins found in any species of bacterium.Protozoan Proteins: Proteins found in any species of protozoan.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Immunoglobulin G: The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Diphtheria Toxin: An ADP-ribosylating polypeptide produced by CORYNEBACTERIUM DIPHTHERIAE that causes the signs and symptoms of DIPHTHERIA. It can be broken into two unequal domains: the smaller, catalytic A domain is the lethal moiety and contains MONO(ADP-RIBOSE) TRANSFERASES which transfers ADP RIBOSE to PEPTIDE ELONGATION FACTOR 2 thereby inhibiting protein synthesis; and the larger B domain that is needed for entry into cells.Membrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.Antigens, Bacterial: Substances elaborated by bacteria that have antigenic activity.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Autoantibodies: Antibodies that react with self-antigens (AUTOANTIGENS) of the organism that produced them.Oncogene Proteins, Fusion: The GENETIC TRANSLATION products of the fusion between an ONCOGENE and another gene. The latter may be of viral or cellular origin.Kinetics: The rate dynamics in chemical or physical systems.Molecular Weight: The sum of the weight of all the atoms in a molecule.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Gene Fusion: The GENETIC RECOMBINATION of the parts of two or more GENES resulting in a gene with different or additional regulatory regions, or a new chimeric gene product. ONCOGENE FUSION includes an ONCOGENE as at least one of the fusion partners and such gene fusions are often detected in neoplastic cells and are transcribed into ONCOGENE FUSION PROTEINS. ARTIFICIAL GENE FUSION is carried out in vitro by RECOMBINANT DNA technology.Spinal Fusion: Operative immobilization or ankylosis of two or more vertebrae by fusion of the vertebral bodies with a short bone graft or often with diskectomy or laminectomy. (From Blauvelt & Nelson, A Manual of Orthopaedic Terminology, 5th ed, p236; Dorland, 28th ed)T-Lymphocytes: Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.ADP Ribose Transferases: Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.DNA, Recombinant: Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected.Green Fluorescent Proteins: Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Membrane Fusion Proteins: Proteins that catalyze MEMBRANE FUSION.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Luminescent Proteins: Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.Bacterial Toxins: Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Maltose-Binding Proteins: Periplasmic proteins that bind MALTOSE and maltodextrin. They take part in the maltose transport system of BACTERIA.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Baculoviridae: Family of INSECT VIRUSES containing two subfamilies: Eubaculovirinae (occluded baculoviruses) and Nudibaculovirinae (nonoccluded baculoviruses). The Eubaculovirinae, which contain polyhedron-shaped inclusion bodies, have two genera: NUCLEOPOLYHEDROVIRUS and GRANULOVIRUS. Baculovirus vectors are used for expression of foreign genes in insects.Viral Envelope Proteins: Layers of protein which surround the capsid in animal viruses with tubular nucleocapsids. The envelope consists of an inner layer of lipids and virus specified proteins also called membrane or matrix proteins. The outer layer consists of one or more types of morphological subunits called peplomers which project from the viral envelope; this layer always consists of glycoproteins.beta-Galactosidase: A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.Recombination, Genetic: Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Cercopithecus aethiops: A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.Viral Proteins: Proteins found in any species of virus.Oncogene Fusion: The GENETIC RECOMBINATION of the parts of two or more GENES, including an ONCOGENE as at least one of the fusion partners. Such gene fusions are often detected in neoplastic cells and are transcribed into ONCOGENE FUSION PROTEINS.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Spodoptera: A genus of owlet moths of the family Noctuidae. These insects are used in molecular biology studies during all stages of their life cycle.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Virus Internalization: The entering of cells by viruses following VIRUS ATTACHMENT. This is achieved by ENDOCYTOSIS, by direct MEMBRANE FUSION of the viral membrane with the CELL MEMBRANE, or by translocation of the whole virus across the cell membrane.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Immunoglobulin Fc Fragments: Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Translocation, Genetic: A type of chromosome aberration characterized by CHROMOSOME BREAKAGE and transfer of the broken-off portion to another location, often to a different chromosome.Pichia: Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.Microscopy, Fluorescence: Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.Genes, Bacterial: The functional hereditary units of BACTERIA.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Mice, Inbred C57BLSequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Vesicular Transport Proteins: A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Giant Cells: Multinucleated masses produced by the fusion of many cells; often associated with viral infections. In AIDS, they are induced when the envelope glycoprotein of the HIV virus binds to the CD4 antigen of uninfected neighboring T4 cells. The resulting syncytium leads to cell death and thus may account for the cytopathic effect of the virus.Vero Cells: A CELL LINE derived from the kidney of the African green (vervet) monkey, (CERCOPITHECUS AETHIOPS) used primarily in virus replication studies and plaque assays.

VEGF is required for growth and survival in neonatal mice. (1/41883)

We employed two independent approaches to inactivate the angiogenic protein VEGF in newborn mice: inducible, Cre-loxP- mediated gene targeting, or administration of mFlt(1-3)-IgG, a soluble VEGF receptor chimeric protein. Partial inhibition of VEGF achieved by inducible gene targeting resulted in increased mortality, stunted body growth and impaired organ development, most notably of the liver. Administration of mFlt(1-3)-IgG, which achieves a higher degree of VEGF inhibition, resulted in nearly complete growth arrest and lethality. Ultrastructural analysis documented alterations in endothelial and other cell types. Histological and biochemical changes consistent with liver and renal failure were observed. Endothelial cells isolated from the liver of mFlt(1-3)-IgG-treated neonates demonstrated an increased apoptotic index, indicating that VEGF is required not only for proliferation but also for survival of endothelial cells. However, such treatment resulted in less significant alterations as the animal matured, and the dependence on VEGF was eventually lost some time after the fourth postnatal week. Administration of mFlt(1-3)-IgG to juvenile mice failed to induce apoptosis in liver endothelial cells. Thus, VEGF is essential for growth and survival in early postnatal life. However, in the fully developed animal, VEGF is likely to be involved primarily in active angiogenesis processes such as corpus luteum development.  (+info)

Cell polarization: chemotaxis gets CRACKing. (2/41883)

An early stage in the establishment of cell polarity during chemotaxis of Dictyostelium dicoideum has been identified by a recent study; the new results also show that the development of cell polarity does not rely upon cytoskeletal rearrangement, and may use a spatial sensing mechanism.  (+info)

Deletion analysis of the Drosophila Inscuteable protein reveals domains for cortical localization and asymmetric localization. (3/41883)

The Drosophila Inscuteable protein acts as a key regulator of asymmetric cell division during the development of the nervous system [1] [2]. In neuroblasts, Inscuteable localizes into an apical cortical crescent during late interphase and most of mitosis. During mitosis, Inscuteable is required for the correct apical-basal orientation of the mitotic spindle and for the asymmetric segregation of the proteins Numb [3] [4] [5], Prospero [5] [6] [7] and Miranda [8] [9] into the basal daughter cell. When Inscuteable is ectopically expressed in epidermal cells, which normally orient their mitotic spindle parallel to the embryo surface, these cells reorient their mitotic spindle and divide perpendicularly to the surface [1]. Like the Inscuteable protein, the inscuteable RNA is asymmetrically localized [10]. We show here that inscuteable RNA localization is not required for Inscuteable protein localization. We found that a central 364 amino acid domain - the Inscuteable asymmetry domain - was necessary and sufficient for Inscuteable localization and function. Within this domain, a separate 100 amino acid region was required for asymmetric localization along the cortex, whereas a 158 amino acid region directed localization to the cell cortex. The same 158 amino acid fragment could localize asymmetrically when coexpressed with the full-length protein, however, and could bind to Inscuteable in vitro, suggesting that this domain may be involved in the self-association of Inscuteable in vivo.  (+info)

Bcl-2 regulates amplification of caspase activation by cytochrome c. (4/41883)

Caspases, a family of specific proteases, have central roles in apoptosis [1]. Caspase activation in response to diverse apoptotic stimuli involves the relocalisation of cytochrome c from mitochondria to the cytoplasm where it stimulates the proteolytic processing of caspase precursors. Cytochrome c release is controlled by members of the Bcl-2 family of apoptosis regulators [2] [3]. The anti-apoptotic members Bcl-2 and Bcl-xL may also control caspase activation independently of cytochrome c relocalisation or may inhibit a positive feedback mechanism [4] [5] [6] [7]. Here, we investigate the role of Bcl-2 family proteins in the regulation of caspase activation using a model cell-free system. We found that Bcl-2 and Bcl-xL set a threshold in the amount of cytochrome c required to activate caspases, even in soluble extracts lacking mitochondria. Addition of dATP (which stimulates the procaspase-processing factor Apaf-1 [8] [9]) overcame inhibition of caspase activation by Bcl-2, but did not prevent the control of cytochrome c release from mitochondria by Bcl-2. Cytochrome c release was accelerated by active caspase-3 and this positive feedback was negatively regulated by Bcl-2. These results provide evidence for a mechanism to amplify caspase activation that is suppressed at several distinct steps by Bcl-2, even after cytochrome c is released from mitochondria.  (+info)

Plasma membrane recruitment of RalGDS is critical for Ras-dependent Ral activation. (5/41883)

In COS cells, Ral GDP dissociation stimulator (RalGDS)-induced Ral activation was stimulated by RasG12V or a Rap1/Ras chimera in which the N-terminal region of Rap1 was ligated to the C-terminal region of Ras but not by Rap1G12V or a Ras/Rap1 chimera in which the N-terminal region of Ras was ligated to the C-terminal region of Rap1, although RalGDS interacted with these small GTP-binding proteins. When RasG12V, Ral and the Rap1/Ras chimera were individually expressed in NIH3T3 cells, they localized to the plasma membrane. Rap1Q63E and the Ras/Rap1 chimera were detected in the perinuclear region. When RalGDS was expressed alone, it was abundant in the cytoplasm. When coexpressed with RasG12V or the Rap1/Ras chimera, RalGDS was detected at the plasma membrane, whereas when coexpressed with Rap1Q63E or the Ras/Rap1 chimera, RalGDS was observed in the perinuclear region. RalGDS which was targeted to the plasma membrane by the addition of Ras farnesylation site (RalGDS-CAAX) activated Ral in the absence of RasG12V. Although RalGDS did not stimulate the dissociation of GDP from Ral in the absence of the GTP-bound form of Ras in a reconstitution assay using the liposomes, RalGDS-CAAX could stimulate it without Ras. RasG12V activated Raf-1 when they were coexpressed in Sf9 cells, whereas RasG12V did not affect the RalGDS activity. These results indicate that Ras recruits RalGDS to the plasma membrane and that the translocated RalGDS induces the activation of Ral, but that Rap1 does not activate Ral due to distinct subcellular localization.  (+info)

B-MYB transactivates its own promoter through SP1-binding sites. (6/41883)

B-MYB is an ubiquitous protein required for mammalian cell growth. In this report we show that B-MYB transactivates its own promoter through a 120 bp segment proximal to the transcription start site. The B-MYB-responsive element does not contain myb-binding sites and gel-shift analysis shows that SP1, but not B-MYB, protein contained in SAOS2 cell extracts binds to the 120 bp B-myb promoter fragment. B-MYB-dependent transactivation is cooperatively increased in the presence of SP1, but not SP3 overexpression. When the SP1 elements of the B-myb promoter are transferred in front of a heterologous promoter, an increased response to B-MYB results. In contrast, c-MYB, the prototype member of the Myb family, is not able to activate the luciferase construct containing the SP1 elements. With the use of an SP1-GAL4 fusion protein, we have determined that the cooperative activation occurs through the domain A of SP1. These observations suggest that B-MYB functions as a coactivator of SP1, and that diverse combinations of myb and SP1 sites may dictate the responsiveness of myb-target genes to the various members of the myb family.  (+info)

A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA. (7/41883)

The nature of the broad substrate specificity phenomenon, as manifested by multidrug resistance proteins, is not yet understood. In the Escherichia coli multidrug transporter, MdfA, the hydrophobicity profile and PhoA fusion analysis have so far identified only one membrane-embedded charged amino acid residue (E26). In order to determine whether this negatively charged residue may play a role in multidrug recognition, we evaluated the expression and function of MdfA constructs mutated at this position. Replacing E26 with the positively charged residue lysine abolished the multidrug resistance activity against positively charged drugs, but retained chloramphenicol efflux and resistance. In contrast, when the negative charge was preserved in a mutant with aspartate instead of E26, chloramphenicol recognition and transport were drastically inhibited; however, the mutant exhibited almost wild-type multidrug resistance activity against lipophilic cations. These results suggest that although the negative charge at position 26 is not essential for active transport, it dictates the multidrug resistance character of MdfA. We show that such a negative charge is also found in other drug resistance transporters, and its possible significance regarding multidrug resistance is discussed.  (+info)

Assembly requirements of PU.1-Pip (IRF-4) activator complexes: inhibiting function in vivo using fused dimers. (8/41883)

Gene expression in higher eukaryotes appears to be regulated by specific combinations of transcription factors binding to regulatory sequences. The Ets factor PU.1 and the IRF protein Pip (IRF-4) represent a pair of interacting transcription factors implicated in regulating B cell-specific gene expression. Pip is recruited to its binding site on DNA by phosphorylated PU.1. PU.1-Pip interaction is shown to be template directed and involves two distinct protein-protein interaction surfaces: (i) the ets and IRF DNA-binding domains; and (ii) the phosphorylated PEST region of PU.1 and a lysine-requiring putative alpha-helix in Pip. Thus, a coordinated set of protein-protein and protein-DNA contacts are essential for PU.1-Pip ternary complex assembly. To analyze the function of these factors in vivo, we engineered chimeric repressors containing the ets and IRF DNA-binding domains connected by a flexible POU domain linker. When stably expressed, the wild-type fused dimer strongly repressed the expression of a rearranged immunoglobulin lambda gene, thereby establishing the functional importance of PU.1-Pip complexes in B cell gene expression. Comparative analysis of the wild-type dimer with a series of mutant dimers distinguished a gene regulated by PU.1 and Pip from one regulated by PU.1 alone. This strategy should prove generally useful in analyzing the function of interacting transcription factors in vivo, and for identifying novel genes regulated by such complexes.  (+info)

*PLGLB2

Characterization of cDNAs and recombinant fusion proteins". Eur. J. Biochem. 259 (3): 618-25. doi:10.1046/j.1432-1327.1999. ... Plasminogen-related protein B is a protein that in humans is encoded by the PLGLB2 gene. GRCh38: Ensembl release 89: ...

*TopoTarget

APO010, also known as mega-FasLigand is a recombinant fusion protein. This protein was derived from the pro-apoptotic human Fas ... APO200 is a therapeutic recombinant protein that is developed from the ectodysplasin A-1 (EDA1) gene. This product is used to ... A current target is Heat Shock Protein 90 (HSP90). HSP90 is key in protein folding and maturation. TopoTarget is currently ... pg 20 The recombinant protein product targets the ErbB2/HER2 receptor, which is overexpressed in 30% of breast cancer and is ...

*Belimumab

Atacicept is a recombinant fusion protein built with the extracellular ligand binding portion of TACI. It blocks activation of ... BR3-Fc is a recombinant fusion protein built with the extracellular ligand-binding portion of BAFF-R. It blocks activation of ... naming the protein TALL-1. The same protein was named BAFF in another paper published in June 1999; and in a paper published in ... isolation of over one thousand different antibodies to a single protein, BLyS". J. Mol. Biol. 334 (1): 103-18. doi:10.1016/j. ...

*Atacicept

... is a recombinant fusion protein designed to inhibit B cells, thereby suppressing autoimmune disease. The designer ... The subcutaneously injected protein failed a phase II trial for multiple sclerosis. The trials of atacicept in people with MS ... a transmembrane receptor protein found predominantly on the surface of B cells. Like the monoclonal antibody belimumab, ... protein combines the binding site for two cytokines that regulate maturation, function, and survival of B cells - B-lymphocyte ...

*Nuclear-inclusion-a endopeptidase

The enzyme is used encoded in vectors for the artificial expression of recombinant fusion proteins (see TEV protease). Fellers ...

*CD4 immunoadhesin

... is a recombinant fusion protein consisting of a combination of CD4 and the fragment crystallizable region. It ... 2007). "Nonlinear pharmacokinetics of high-dose recombinant fusion protein CD4-IgG2 (PRO 542) observed in HIV-1-infected ... CD4 is a surface receptor for human immunodeficiency virus (HIV). The properties of the protein means that it has potential to ...

*TEV protease

One of the main uses of this protein is for removing affinity tags from purified recombinant fusion proteins. The reason for ... "Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase". Anal. Biochem. 216 (2): 413- ... Kapust RB, Waugh DS (July 2000). "Controlled intracellular processing of fusion proteins by TEV protease". Protein Expr. Purif ... Due to its high sequence specificity it is frequently used for the controlled cleavage of fusion proteins in vitro and in vivo ...

*Human metapneumovirus

... on the Basis of a Novel Enzyme-Linked Immunosorbent Assay Utilizing hMPV Fusion Protein Expressed in Recombinant Vesicular ... Determined with a New Recombinant Fusion Protein Enzyme-Linked Immunosorbent Assay". Clinical and Vaccine Immunology. 20 (10): ... The HMPV fusion (F) protein encodes an RGD (Arg-Gly-Asp) motif that engages RGD-binding integrins as cellular receptors, then ... "Human Metapneumovirus Reinfection among Children in Thailand Determined by ELISA Using Purified Soluble Fusion Protein". The ...

*Albinterferon

... (alb-IFN, trade name Albuferon) is a recombinant fusion protein drug consisting of interferon alpha (IFN-α) ... November 2002). "Pharmacokinetic and pharmacodynamic studies of a human serum albumin-interferon-alpha fusion protein in ...

*Ruth Sonntag Nussenzweig

"TLR5-dependent immunogenicity of a recombinant fusion protein containing an immunodominant epitope of malarial circumsporozoite ... "Human immune system mice immunized with Plasmodium falciparum circumsporozoite protein induce protective human humoral immunity ... "Antibodies to Plasmodium circumsporozoite protein (CSP) inhibit sporozoite's cell traversal activity." Journal of Immunological ... "Immunogenicity of a Prime-Boost Vaccine Containing the Circumsporozoite Proteins of Plasmodium vivax in Rodents. Infection and ...

*Luspatercept

... is a recombinant fusion protein derived from human activin receptor type IIb (ActRIIb) linked to a protein derived ...

*BDH1

... site-directed mutagenesis of a new recombinant fusion protein". Biochemistry. 39 (32): 9687-97. doi:10.1021/bi000274z. PMID ... The encoded protein forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific requirement ... The encoded protein catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the two major ketone bodies ... Alternatively spliced transcript variants encoding the same protein have been described. 3-hydroxybutyrate dehydrogenase ...

*IMP321

... is a 200 kDA soluble dimeric recombinant fusion protein of the extracellular portion of LAG3 with immunoglobulin, ... Li B, VanRoey M, Triebel F, Jooss K (June 1, 2008). "Lymphocyte activation gene-3 fusion protein increases the potency of a ... had successfully produced a soluble fusion protein of LAG3 and immunoglobulin around 1995 and had initially envisaged its use ... LAG-3Ig fusion protein) in patients receiving autologous PBMCs after lymphodepletion: results of a Phase I trial". J Transl Med ...

*Transmembrane activator and CAML interactor

TACI is currently being targeted for autoimmunity and B cell malignancies via atacicept, a recombinant fusion protein that ... is a protein that in humans is encoded by the TNFRSF13B gene TNFRSF13B is a transmembrane protein of the TNF receptor ... These proteins signal through TACI inducing activation of several transcription factors including NFAT, AP-1, and NF-kappa-B ... In humans, the gene encoding this protein is located within the Smith-Magenis syndrome region on chromosome 17. ...

*Thrombin

... is commonly included in linker regions of recombinant fusion protein constructs. Following purification of the fusion protein, ... Activated protein C inactivates factors Va and VIIIa. Binding of activated protein C to protein S leads to a modest increase in ... Thrombin bound to thrombomodulin activates protein C, an inhibitor of the coagulation cascade. The activation of protein C is ... Recombinant thrombin is available as a powder for reconstitution into aqueous solution. It can be applied topically during ...

*Immunotoxin

Sometimes recombinant fusion proteins containing a toxin and a growth factor are also referred to as recombinant immunotoxins, ... A more specific name for this latter kind of protein is recombinant fusion toxin. They were originally produced by attaching ... An immunotoxin is a human-made protein that consists of a targeting portion linked to a toxin. When the protein binds to that ... The toxin is usually a cytotoxic protein derived from a bacterial or plant protein, from which the natural binding domain has ...

*Interleukin 2

Eisai markets a drug called denileukin diftitox (trade name Ontak), which is a recombinant fusion protein of the human IL-2 ... Amgen later entered the field with its own proprietary, mutated, recombinant protein and Cetus and Amgen were soon competing ... Aldesleukin is a form of recombinant interleukin-2. It is manufactured using recombinant DNA technology and is marketed as a ... Interking is a recombinant IL-2 with a serine at residue 125, sold by Shenzhen Neptunus. Various dosages of IL-2 across the ...

*Dendritic cells- based cancer vaccines

The cells are incubated ex vivo in the presence of a recombinant fusion protein PA2024 containing a prostate antigen, prostate ... We can used specific TAAs, tumor lysates,created DC-cancer cell fusions, electroporation/transfection of DCs with total cancer ...

*EGTA (chemical)

... in which recombinant fusion proteins are bound to calmodulin beads and eluted out by adding EGTA. EGTA is often employed in ... EGTA is used as a compound in elution buffer in the protein purification technique known as tandem affinity purification, ...

*Aflibercept

... is a recombinant fusion protein consisting of vascular endothelial growth factor (VEGF)-binding portions from the ... leading to blood and protein leakage below the macula. Tumours need blood vessels sprouting into them when they become larger ...

*Protein A/G

... is a recombinant fusion protein that combines IgG binding domains of both Protein A and Protein G. Protein A/G ... In addition to Protein A/G, other immunoglobulin-binding bacterial proteins such as Protein A, Protein G and Protein L are all ... The binding of Protein A/G is less pH-dependent than Protein A, but otherwise has the additive properties of Protein A and G. ... Mouse monoclonal antibodies commonly have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G ...

*Fusion protein

A recombinant fusion protein is a protein created through genetic engineering of a fusion gene. This typically involves ... Examples include: Gag-onc fusion protein Bcr-abl fusion protein Tpr-met fusion protein Antibodies are fusion proteins produced ... Recombinant fusion proteins are created artificially by recombinant DNA technology for use in biological research or ... The bcr-abl fusion protein is a well-known example of an oncogenic fusion protein, and is considered to be the primary ...

*Factor IX

Recombinant), Fc Fusion Protein] Official Site". Simioni P, Tormene D, Tognin G, Gavasso S, Bulato C, Iacobelli NP, Finn JD, ... The factor IX protein is composed of four protein domains: the Gla domain, two tandem copies of the EGF domain and a C-terminal ... Deficiency of this protein causes hemophilia B. It was discovered in 1952 after a young boy named Stephen Christmas was found ... A structure of the two EGF domains and the trypsin-like domain was determined for the pig protein. The structure of the Gla ...

*Etanercept

... is a fusion protein produced by recombinant DNA. It fuses the TNF receptor to the constant end of the IgG1 antibody ... Finally, they expressed the linked DNA to produce a protein that links the protein for TNF receptor 2 to the protein for IgG1 ... The prototypic fusion protein was first synthesized and shown to be highly active and unusually stable as a modality for ... The effect is an artificially engineered dimeric fusion protein. Etanercept is a complex molecules containing 6 N-glycans, up ...

*TROVE2

1990). "Antigenicity of a recombinant Ro (SS-A) fusion protein". Arthritis Rheum. 33 (1): 102-6. doi:10.1002/art.1780330114. ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ... 60 kDa SS-A/Ro ribonucleoprotein is a protein that in humans is encoded by the TROVE2 gene. GRCh38: Ensembl release 89: ... 2005). "RNA chaperone activity of protein components of human Ro RNPs". RNA. 11 (7): 1084-94. doi:10.1261/rna.7263905. PMC ...

*Phage display

Many genetic sequences are expressed in a bacteriophage library in the form of fusions with the bacteriophage coat protein, so ... "Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro". Proc. Natl. Acad. Sci. U.S.A. 89 (19 ... Phage display is a laboratory technique for the study of protein-protein, protein-peptide, and protein-DNA interactions that ... a gene encoding a protein of interest is inserted into a phage coat protein gene, causing the phage to "display" the protein on ...
Protein drug delivery is limited to needle injection associating with pain, inconvenience, and non- compliance. Therefore, protein drug with oral dosage form is preferred. We used transferrin (Tf) receptor mediated transcytosis and Tf-based recombinant fusion protein approach to achieve oral delivery of human growth hormone (hGH). Plasmid constructs expressing the fusion proteins were established by fusing coding sequences of both hGH and Tf in frame. Fusion proteins were produced in serum free media by transcient transfection of human embryonic kidney cells. The SDS-PAGE of conditioned media showed that fusion proteins expressed at ~ 90% abundance and 100 kDa molecular weight; the Western blot analysis with anti-hGH and anti-Tf antibodies verified the identity. The Nb2 cell proliferation and TfR binding assays demonstrated that fusion proteins retained bioactivity for both hGH and Tf, respectively. To minimize inter-domain interference, we inserted 2 copies of helical linker as a spacer between ...
Thesis, English, Studying the role of rhBAFF and BAFF R Fc fusion protein on lymphocytes and platelets in patients with immune thrombocytopenia for Nouran Mohamed Nabil Momen
Dear netters, I am a PhD student in Japan. I am facing some problems in expressing my fusion proteins (both GST-fusions and His-tag fusions) in soluble fractions; therefore I decided to use the TNT-coupled recticulocyte system to synthesis the desired proteins. I need to use these fusion proteins for the following assay: (i) protein interaction - pull down assay (ii) in-vitro kinase assay My questions are: (i) how to purify the translated product from the TNT- coupled recticulocyte system? (ii) Are there any references for the above assays (pull down assay & in-vitro kinase assay) using both in-vitro translated fusion proteins? Your help are kindly appreciated. Thank you. sincerely, YK ...
Two murine Mabs VA1(IgG1) and VA2(IgG1) were produced against a bacterial fusion protein comprising glutathione S-transferase and five tandem repeats of the MUC1 protein. Using the immunoperoxidase staining technique, VA1 detected 46/53 and VA2 detected 48/53 breast cancers and both also reacted wit...
The invention relates to novel recombinant fusion proteins comprising two or more erythropoietin molecules. The fusion proteins can be linked by a peptide linker. The fusion proteins can be used, for example, to treat or prevent anemia in a mammal. Also disclosed are nucleotide sequences encoding the fusion proteins vectors comprising the nucleic acid sequences of the fusion proteins and host cells transfected with the vectors.
The FLAG Expression System is an established way to express, purify and detect recombinant fusion proteins. FLAG and 3xFLAG have proven utility in numerous applications such as Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure and protein localization. These small hydrophilic tags facilitate superior detection and purification of recombinant fusion proteins when using our highly specific and sensitive ANTI-FLAG® antibodies. Ideal epitope tags are small, hydrophilic and cleavable.. The FLAG expression system utilizes a short, hydrophilic 8-amino acid peptide that is fused to the recombinant protein of interest. Because of its hydrophilic nature, the FLAG peptide is likely to be located on the surface of the fusion protein. As a result, the FLAG peptide is easily accessible for cleavage by enterokinase (Ek) and for detection with antibodies. In addition, because of the small size ...
Purification tags/Protein tag,Protein tags are peptide sequences genetically grafted onto a recombinant protein. Often these tags are removable by chemical agents or by enzymatic means, such as proteolysis or intein splicing. Tags are attached to proteins for various purposes.
Recombinant soluble human glycoprotein Ib alfa-Ig fusion protein consists of the amino-terminal 290 amino acids of glycprotein (GP) Ibα and a mutated human IgG1
Sigma-Aldrich offers abstracts and full-text articles by [Fabio Vanoli, Mark Tomishima, Weiran Feng, Khadija Lamribet, Loelia Babin, Erika Brunet, Maria Jasin].
Human C12orf5 (Q9NQ88) full-length recombinant protein C-termial fused to TAT peptide (GGGYGRKKRRQRRR) expressed in Escherichia coli. (P6037) - Products - Abnova
Website: http://labs.fhcrc.org/strong/. Tailoring immunotargeting and immunomodulatory reagents for the treatment of cancer. This project builds on two ongoing efforts: (1) to specifically elicit, customize and weaponize antibodies to target solid tumors induced by viruses and (2) to translate immunomodulators that target T cell co-receptor signaling pathways from canine to human patients for managing the sequelae of treatments for hematopoietic tumors. Antibodies are clinically-relevant reagents for treating various diseases, though often require chemical conjugation to generate useful diagnostics or therapeutics. We are developing novel antibody fusion proteins, adding functional modules that enable simple, plug-and-play, non-covalent incorporation of a variety of adducts. We are also developing improved versions of MHC proteins as immunogens to efficiently elicit antibodies specific for virally-infected cells. Computational refinement of initial designs is required to fully realize these ...
The present invention provides humanized, chimeric and human anti-CD74 antibodies, CD74 antibody fusion proteins, immunoconjugates, vaccines and bispecific that bind to CD74, the major histocompatibil
i want to understand also how to determine which OD to start my IPTG induction in? and when to say its time to stop when OD reaches 2 ...
I clone GST fusion proteins with pGEX 4T-3 vector, I check for inserts in minipreps (OK), grow bacteria, induce them, and run lysates on SDS-PAGE. What happens is that the expressed proteins are of GST size, probably degraded. Has anyone got that kind of results before? I checked DNA, its OK, no stop codons at the ligation site.. ...
I am attemptting to make a monoclonal antibody aganist a GST fusion protein ( 34 kDa). I am wondering if anybody outthere can tell me how much purified antigen I need to use for each immunization, and how much antigen I have to use for coding the plates for screening. Thank you, Qiang ...
Since many years Chimerigen Laboratories, LLC (Chimerigen) develops, manufactures and markets high quality and leading edge proteins for biomedical and immunology research. One of Chimerigens specialty is the production of unique immunoglobulin based chimeric fusion proteins using advanced cellular and molecular biological techniques.
The ERM proteins, ezrin, radixin, and moesin, are involved in the actin filament/plasma membrane interaction as cross-linkers. CD44 has been identified as one of the major membrane binding partners for ERM proteins. To examine the CD44/ERM protein interaction in vitro, we produced mouse ezrin, radixin, moesin, and the glutathione-S-transferase (GST)/CD44 cytoplasmic domain fusion protein (GST-CD44cyt) by means of recombinant baculovirus infection, and constructed an in vitro assay for the binding between ERM proteins and the cytoplasmic domain of CD44. In this system, ERM proteins bound to GST-CD44cyt with high affinity (Kd of moesin was 9.3 +/- 1.6nM) at a low ionic strength, but with low affinity at a physiological ionic strength. However, in the presence of phosphoinositides (phosphatidylinositol [PI], phosphatidylinositol 4-monophosphate [4-PIP], and phosphatidylinositol 4.5-bisphosphate [4,5-PIP2]), ERM proteins bound with a relatively high affinity to GST-CD44cyt even at a physiological ...
RATIONALE: Targeted therapy with tumor necrosis factor combined with a fusion protein may stop the growth of solid tumors by stopping blood flow to the
Human VISTA / B7-H5 / PD-1H protein (7126-B7) is manufactured by R&D Systems, over 95% purity. Reproducible results in bioactivity assays. Learn More...
new growths elsewhere in the body, a process known as metastasis that can cause cancer to spread with deadly effect, the findings showed. "This is a very promising therapy that appears to be effective and non-toxic in pre-clinical experiments," said co-researcher Amato Giaccia, a professor at the Stanford University in the US. "It could open up a new approach to cancer treatment," Giaccia added. Today doctors try to slow or stop metastasis with chemotherapy, but these treatments are unfortunately not very effective and have severe side effects. The researchers sought to stop metastasis by preventing two proteins - Axl and Gas6 - from interacting to initiate the spread of cancer. Axl proteins stand like bristles on the surface of cancer cells, poised to receive bio-chemical signals from Gas6 proteins. When two Gas6 proteins link with two Axls, the signals that are generated enable cancer cells to leave the original tumor site, migrate to other parts of the body and form new cancer nodules ...
In a preclinical study, researchers at the University of Southern California evaluated whether human Collagen 7 that had been produced in the lab, when applied to mouse skin, could restore the missing protein in the skin and enhance wound healing.. They found that the Collagen 7 applied to the surface of the mouse skin was incorporated stably at the newly formed junction between the dermis and epidermis of healed wounds. It accelerated wound closure by increasing the formation of new epithelium (skin). It also led to reduced scarring and had other positive impacts. ...
Gentaur molecular products has all kinds of products like :search , Clemente Associates Inc \ FUSION PROTEIN TAGS Anti FLAG M1 \ flgm1250 for more molecular products just contact us
Studying the role of the fusion protein MLL-AF4 in leukemogenesis with the help of siRNAs [Elektronische Ressource] / von Maria Thomas (geb. Arkhipova) : Studying the role of the fusion protein MLL-AF4 in leukemogenesis with the help of siRNAs der Fakultät für Biologie der Eberhard Karls Universität Tübingen zur Erlangung des Grades eines Doktors der Naturwissenschaften von Maria Thomas (geb. Arkhipova) aus Pushchino (Russland) vorgelegte D i s s e r t a t i o n 2007 Tag der mündlichen Prüfung: 11.10
CGEN-15001T is a novel B7/CD28-like immune checkpoint target candidate discovered by Compugen.. Studies testing the immune function of CGEN-15001T, as a membrane bound protein or using a recombinant fusion protein containing the extracellular domain of CGEN-15001T, showed it is capable of inhibiting T cell activation, promoting a Th1 to Th2 shift, and potentially inducing immune tolerance. CGEN-15001T is expressed in subpopulations of immune cells, mainly macrophages, in both tumor and normal tissue samples.. In August 2013, Compugen signed a research and discovery collaboration and license agreement with Bayer HealthCare for the development and commercialization of antibody-based therapeutics for cancer immunotherapy against CGEN-15001T. After achieving all preclinical stage milestones, this program was transferred to Bayer for further development. To date, preclinical activities are on track, and pivotal toxicity studies and GMP clinical trial material production are ongoing.. ...
Rabbit polyclonal Ran antibody validated for WB, ICC/IF. Referenced in 2 publications. Immunogen corresponding to recombinant fusion protein
Mouse monoclonal Livin antibody [88C570] validated for WB, Flow Cyt and tested in Human. Immunogen corresponding to recombinant fusion protein
Many leukemias begin when a large piece of one chromosome becomes loose and reattaches to another chromosome. This can produce fusion proteins that shut down DNA repair gens and activate genes that help the cells proliferate.
P27; KIP1 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag2280
In vivo degradation of GFP and a GFP-HipB hybrid.GFP and GFP with C-terminal fusion to the C terminus of HipB were expressed from a pBRlacitac promoter in BW251
Nine different IgG fusion proteins and one non-fusion protein, all containing sequences from the extracellular domain of either of two human TNF receptors, were compared for their ability to bind and inhibit human TNF-alpha or TNF-beta. The fusion proteins differed with respect to TNF receptor type (p55 or p75 TNF receptor), receptor valency (one, two or four receptor domains per molecule), the presence or absence of a CH1 domain in the IgG constant region, and the proportion of the extracellular domain included in the construct. In vitro TNF binding assays and cytotoxicity assays indicated that, of the constructs that bound TNF, the greatest difference in affinity and neutralizing capability was between monovalent and bivalent receptor constructs. Differences were also noted between tetravalent and bivalent versions of p55 fusion proteins, as well as between a p75 fusion protein comprising the complete extracellular domain and one lacking the C-terminal 53 amino acids of the extracellular domain. p55
Recombinant fusion proteins have become an important class of biomolecules since the invention of recombinant DNA technology. As an indispensable component of recombinant fusion proteins, linkers have shown increasing importance in the construction of stable, bioactive fusion proteins. In the development of recombinant transferrin (Tf)-fusion proteins for protein drug oral delivery, various linkers have been designed to improve the biological activity, or to achieve desired pharmacokinetic and pharmacodynamic properties. ❧ The Introduction in this dissertation first reviewed the mechanism for Tf receptor-mediated protein drug oral delivery, as well as the recombinant Tf-fusion proteins that have been constructed previously in our lab. It also covers the current knowledge of fusion protein linkers and summarizes examples for their applications. The basic function of linkers is to covalently join the functional domains in the fusion proteins. However, linkers can offer many other advantages for ...
Recombinant fusion proteins have become an important class of biomolecules since the invention of recombinant DNA technology. As an indispensable component of recombinant fusion proteins, linkers have shown increasing importance in the construction of stable, bioactive fusion proteins. In the development of recombinant transferrin (Tf)-fusion proteins for protein drug oral delivery, various linkers have been designed to improve the biological activity, or to achieve desired pharmacokinetic and pharmacodynamic properties. ❧ The Introduction in this dissertation first reviewed the mechanism for Tf receptor-mediated protein drug oral delivery, as well as the recombinant Tf-fusion proteins that have been constructed previously in our lab. It also covers the current knowledge of fusion protein linkers and summarizes examples for their applications. The basic function of linkers is to covalently join the functional domains in the fusion proteins. However, linkers can offer many other advantages for ...
In the present study, we developed, for the first time, a successful protocol for expression human gAd-GLP-1-A fusion protein from Escherichia coli strain BL21 (DE3). Plasmid vector PET28a was used to express this fusion protein. This vector can produce an N-terminal His-tagged protein. His-tag is often used for protein purification [11]. The affinity of the His-tag for metal ions allows the fusion product to be quickly separated from the bulk of other bacterial proteins by using metal chelate affinity chromatography [11]. Because N-terminal His-tag may influence the function of protein, we designed an enterokinase cleavage site at the 5 terminus of the gene of the gAd-GLP-1-A fusion protein, which was used to remove the His-tag [9]. In our study, most of the His-tagged fusion protein expressed from BL21 (DE3) was present in inclusion body. In order to recover its function, the fusion protein in inclusion body was refolded in urea gradient refolding buffer. And then, the refolded protein was ...
In the present study, using novel fusion proteins, we have demonstrated both constitutive expression of cell surface-tethered hirudin and stimulation-dependent relocation of hirudin from secretory granules to the cell surface. Linked to an appropriate mammalian signal sequence and membrane anchor, hirudin was expressed at the cell surface, where it bound exogenous thrombin via its active site and inhibited the formation of fibrin in an in vitro clotting assay that used human plasma. When the C-terminal sequence of the hirudin-CD4 fusion protein was replaced by a targeting sequence derived from P-selectin, it accumulated in storage granules of secretory cells and could be relocated to the cell surface on activation. Furthermore, this relocated hirudin was active, because specific thrombin binding could be visualized by flow cytometry.. The targeting and regulated expression of the P-selectin-tagged fusion protein were predictable from recent data concerning the intracellular processing of ...
Expression In Bacteria Of Beta-Galactosidase Fusion Proteins Carrying Antigenic Determinants Of The 2 X-Gene Products Of Bovine Leukemia- ...
Fusion of the SS18 and either one of the SSX genes is a hallmark of human synovial sarcoma. The SS18 and SSX genes encode nuclear proteins that exhibit opposite transcriptional activities. The SS18 protein functions as a transcriptional coactivator and is associated with the SWI/SNF complex, whereas the SSX proteins function as transcriptional corepressors and are associated with the polycomb complex. The domains involved in these opposite transcriptional activities are retained in the SS18-SSX fusion proteins. Here, we set out to determine the direct transcriptional consequences of conditional SS18-SSX2 fusion protein expression using complementary DNA microarray-based profiling. By doing so, we identified several clusters of SS18-SSX2-responsive genes, including a group of genes involved in cholesterol synthesis, which is a general characteristic of malignancy. In addition, we identified a group of SS18-SSX2-responsive genes known to be specifically deregulated in primary synovial sarcomas, ...
Detection of Protein-Protein Interactions Using the GST Fusion Protein Pull-down Technique. Bacterially expressed glutathione S-transferase (GST)-fused proteins are used as probes to perform direct measure of protein-protein interactions and for affinity purification. Slideshow 6521621 by...
The potential utility of immunotoxins for cancer therapy has convincingly been demonstrated in clinical studies. Nevertheless, the high immunogenicity of their bacterial toxin domain represents a critical limitation, and has prompted the evaluation of cell-death inducing proteins of human origin as a basis for less immunogenic immunotoxin-like molecules. In this review, we focus on the current status and future prospects of targeted fusion proteins for cancer therapy that employ granzyme B (GrB) from cytotoxic lymphocytes as a cytotoxic moiety. Naturally, this serine protease plays a critical role in the immune defense by inducing apoptotic target cell death upon cleavage of intracellular substrates. Advances in understanding of the structure and function of GrB enabled the generation of chimeric fusion proteins that carry a heterologous cell binding domain for recognition of tumor-associated cell surface antigens. These hybrid molecules display high selectivity for cancer cells, with cell killing
A transferrin-based fusion protein, proinsulin-transferrin (ProIns-Tf) had been constructed using recombinant protein technology in our laboratory. Based on the in vitro preliminary results, ProIns-Tf reduced glucose production in H4IIE liver cells and increased glucose uptake in adipocytes. These potent effects were achieved by conversion of the ProIns moiety to an active Ins-like moiety through the mechanism of TfR-mediated endocytosis. Therefore, ProIns-Tf showed great potential for diabetes therapeutics. However, it was also observed that the preparation of this fusion protein also produced a large amount of protein impurities which might have impeding effects on the further characterization studies. ❧ In this report, ProIns-Tf fusion protein was purified using the polyhistidine tag technique. The hexahistidine tag (6xHis tag) was bound to the C-terminus of Tf domain through mutagenic polymerase chain reaction (PCR) and recombinant DNA technology. After the protein expression and ...
Embodiments of the present invention provide for the facile generation of a stable recombinant fusion polypeptides with intrinsic fluorescent properties. The recombinant antibodies may be suitable fo
Disclosed are compositions and methods for producing fusion proteins with reduced immunogenicity. Fusion proteins of the invention include a junction region having an amino acid change that reduces the ability of a junctional epitope to bind to MHC Class II, thereby reducing its interaction with a T-cell receptor. Methods of the invention involve analyzing, changing, or modifying one or more amino acids in the junction region of a fusion protein in order to identify a T-cell epitope and reduce its ability to interact with a T cell receptor. Compositions and methods of the invention are useful in therapy.
This protocol describes the production of GST-Cbx7 fusion proteins from E. coli, originally developed in the recent publication (Zhen et al., 2016). The pGEX-6P-1-GST plasmids encoding the Cbx7 variants were transformed into BL21 competent cells. The fusion protein production was induced by isopropyl-beta-D-thiogalactopyranoside and they were purified by Glutathione Sepharose 4B. This protocol can be adapted for the purification of other proteins.
[Objective] This study investigates the functional comparison between the diphtheria toxin before the RGD peptide receptor deletion build 391 amino acid (DAB391) of recombinant fusion gene expression
Transfection of the different EGFP fusion constructs to IMR-90 fibroblasts. A) The wild-type SAP30L concentrates in small dense bodies in the nuclei. B) The nuc
A novel biopharmaceutical, consisting of the F8 mAb (specific to a splice isoform of fibronectin) simultaneously fused to both TNF and IL2, was found to react with the majority of solid tumors and hematologic malignancies in mouse and man, but not with healthy adult tissues. The product selectively localized to neoplastic lesions in vivo, as evidenced by quantitative biodistribution studies using radioiodinated protein preparations. When the potency of the cytokine payloads was matched by a single-point mutation, the resulting fusion protein (IL2-F8-TNFmut) eradicated soft-tissue sarcomas in immunocompetent mice, which did not respond to individual antibody-cytokine fusion proteins or by standard doxorubicin treatment. Durable complete responses were also observed in mice bearing CT26, C1498, and F9 tumors. The simultaneous delivery of multiple proinflammatory payloads to the cancer site conferred protective immunity against subsequent tumor challenges. A fully human homolog of IL2-F8-TNFmut, ...
Mouse monoclonal antibody raised against partial recombinant Cntnap1. Recombinant fusion protein corresponding to amino acids of 1308-1381 at cytoplasmic domain of rat Cntnap1. (MAB11892) - Products - Abnova
Protein A affinity chromatography is traditionally used as the capture step for monoclonal antibodies (MAbs) (1,2,3). It yields high purity because only the fragment-crystallizable (Fc) region of an antibody (IgG1 or IgG2) or Fc-containing fusion protein can bind to the protein A ligand. The resulting specificity provides substantial reduction in impurities such as host cell proteins (HCPs) and DNA (4,5,6,7,8). The dynamic binding capacity of protein A chromatography resins is generally ≤40 g/L and depends highly on residence time because…. ...
Protein A affinity chromatography is traditionally used as the capture step for monoclonal antibodies (MAbs) (1,2,3). It yields high purity because only the fragment-crystallizable (Fc) region of an antibody (IgG1 or IgG2) or Fc-containing fusion protein can bind to the protein A ligand. The resulting specificity provides substantial reduction in impurities such as host cell proteins (HCPs) and DNA (4,5,6,7,8). The dynamic binding capacity of protein A chromatography resins is generally ≤40 g/L and depends highly on residence time because…. ...
Caltag Medsystems supply a wide range of fusion proteins for cancer research, neurobiology, metabolism, apoptosis, cell biology, immunology, infectious diseases
... Designation: pTB TypeStrain=False Application: expression vector shuttle vector vector permitting construction of fusion proteins vector permitting visual detection of recombinants
ATCC ® 87059™ Designation: pETGEXCT TypeStrain=False Application: encodes removable tag for protein isolation expression vector vector permitting RNA synthesis in vitro vector permitting construction of fusion proteins
Despite the advances toward the elimination of leprosy through widespread provision of multi-drug therapy to registered patients over the last 2 decades, new case detection rates have stabilized and leprosy remains endemic in a number of localized regions. A vaccine could overcome the inherent limitations of the drug treatment program by providing protection in individuals who are not already harboring the Mycobacterium leprae bacilli at the time of administration and effectively interrupt the transmission cycle over a wider timespan. In this report we present data validating the production of 73f, a chimeric fusion protein incorporating the M. leprae antigens ML2028, ML2346 and ML2044. The 73f protein was recognized by IgG in multibacillary (MB) leprosy patient sera and stimulated IFNγ production within whole blood assays of paucibacillary (PB) leprosy patient and healthy household contacts of MB patients (HHC). When formulated with a TLR4L-containing adjuvant (GLA-SE), 73f stimulated a strong ...
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P. Didier, L. Guidoni, and E. Weiss, "Ultrafast Excited-state Dynamics of Genetic Fusions: The Green Fluorescent Protein as a Folding Reporter," in Conference on Lasers and Electro-Optics/Quantum Electronics and Laser Science Conference and Photonic Applications Systems Technologies, Technical Digest (CD) (Optical Society of America, 2006), paper QMH1 ...
To investigate structure/function relationships involved in the delivery of the diphtheria toxin (DT) catalytic (C) domain to the cytosol of target cells, we have constructed and characterized internal in-frame deletion mutants in the transmembrane (T) domain of the fusion toxin DAB389IL-2. This fusion protein is composed of the C and T domains of DT to which human interleukin-2 (IL-2) has been genetically fused. The mutant fusion toxins were compared to DAB389IL-2 with respect to cytotoxic potency, receptor binding affinity, channel formation in planar lipid membranes, and sensitivity to proteolytic digestion. We demonstrate that genetic fusion of human IL-2 sequences to a diphtheria toxin-related fragment that contains less than full-length transmembrane helix 9 results in a fusion protein that binds to the high affinity IL-2 receptor, but has lost | or = 3 logs of cytotoxic potency and has decreased ability to insert into planar membranes and form stable channels. These observations are consistent
1111674DNAArtificial Sequencesynthetic humanized monoclonal antibody 1actagtaaac gcggtggcgg tgatattcaa atgacacaat ctccttcttc tctgtcagcc 60tcagtgggcg accgtgtgac gattacttgc cgcgcctctc aggacgttaa cactgccgtc 120gcatggtacc agcagaagcc aggcaaggcg cccaagcttc tgatttacag cgcttcgttc 180ctgtactctg gcgtgccatc ccgcttctct ggcagccgaa gcggcacgga tttcaccctg 240accatttcgt ccctgcagcc cgaggatttc gccacgtatt actgccagca gcactacacc 300actccaccca cctttggcca aggaacgaga gtcgaaatca ctcgcacggt cgctgcccct 360tcagtcttca tcttcccccc cagcgacgaa cagctgaagt ctggtacggc cagcgtcgtt 420tgcttgctta ataacttcta tccgcgagag gcgaaggtcc aatggaaggt tgataacgtt 480ctgcagtccg gcaattcgca ggagagcgtg accgagcagg attcaaagga tagcacctac 540tcactcagca gcaccctgac gttgtccaag gccgattacg agaagcataa gttgtatgca 600tgcgaggtca cccaccaggg actgtcaagc ccagttacca agtcgttcaa tcgaggcgag 660tgctaaggcg cgcc 67425PRTArtificial Sequencesynthetic KEX2 variant 2Lys Arg Gly Gly Gly1 5345DNAArtificial SequenceSynthetic oligonucleotide 3ggactagtgg tggcggtaaa cgcgatattc ...
Our researchers have developed a new technology that allows for the study of protein structure/folding/functions in the living cells. This new technology involves expressing a protein using bacteria and labeling the protein with probes. Researchers can then modify the recombinant protein with a special reagent that allows for the transfer of the modified protein into the living mammalian cells. This will also allow for the study of protein traffic in the cells. Furthermore, this new technology permits high-resolution structural biology techniques to be combined with cell biology techniques and provides a foundation for future applications of protein transduction technology, atomic resolution cell biology, and protein drug therapy to treat human disease. ...
3020 A variety of human carcinoma cells express high levels of interleukin-13 receptorα2 chain, a primary binding subunit of IL-13R complex in vitro and in vivo. These receptors could be targeted by a chimeric fusion protein consisting of Interleukin-13 and a truncated form of Pseudomonas exotoxin (IL-13PE38). Microarray analysis of adrenomedullin (AM) transfected human prostate tumor PC-3 cells showed that human and rat AM up-regulated the IL-13Rα2 chain gene. We now demonstrate that IL-13Rα2 chain is also up regulated in two human breast tumor cell lines (MCF-7 and MDA-MB-231) and one prostate carcinoma (PC-3) cell line after treatment with AM. RT-PCR results confirmed that mRNAs for IL-13Rα2 were enhanced 2.5 to 4 fold in 24 and 48 hr AM treated cells, respectively compared to control cells. Indirect immunofluorescence assay (IFA) revealed that protein level of IL-13Rα2 were also increased in AM treated breast and prostate carcinoma cells. To understand the mechanism of up-regulation, ...
Nucleoporin 98 (NUP98) fusions have been associated with acute myeloid leukemia (AML), chronic myeloid leukemia, myelodysplastic syndrome, and T-cell acute lymphoblastic leukemia (T-ALL). An AML patient with a t(11;17)(p15;p13) chromosome translocation was found to have a novel gene fusion between NUP98 and plant homeodomain (PHD) finger 23 (PHF23). PHF23 has been reported to act as a reader of tri-methylated histone 3 lysine 4 (H3K4me3) marks, suggesting that PHF23 may function in chromatin regulation and that the NP23 fusion protein may play a role in aberrant chromatin modification. To determine the oncogenic potential of NP23, we generated mice that expressed the NP23 fusion in hematopoietic tissues.. We characterized two founder lines (C10 and B10) that expressed the NP23 fusion. The C10 line principally developed AML that closely resembled the human disease, with increased blasts in the blood and bone marrow, widespread organ infiltration, and myeloid immunophenotype. Onset of disease was ...
We report for the first time the rela time non-invasive kinetic analysis of three steps in the NF-κB signalling pathway; IκBα degradation, p65 translocation and NF-κB-dependent transcription. We have used these tools to investigate the link between the kinetics of the NF-κB pathway, the levels of NF-κB and IκB proteins in cell compartments, and the resulting timing of transcription.. We showed that both the p65-EGFP and p65-dsRed fluorescent fusion proteins gave rise to the nuclear translocation in response to TNFα treatment, which is characteristic of the functional endogenous protein. Ding et al. previously reported an endogenous p65 nuclear translocation half time of 7-8 minutes in HeLa cells following TNFα stimulation ( Ding et al., 1998). In comparison, we obtained a longer half time of 19±2.9 minutes for nuclear translocation of p65-EGFP in singly transfected cells ( Fig. 1A) in agreement with other studies using a p65-EGFP fluorescent fusion protein and stimulation with IL-1β ( ...
Understanding the cell biology of many proteins requires knowledge of their in vivo topological distribution. Here we describe a new fluorescence-based technique, fluorescence protease protection (FPP), for investigating the topology of proteins and for localizing protein subpopulations within the complex environment of the living cell. In the FPP assay, adapted from biochemical protease protection assays, GFP fusion proteins are used as noninvasive tools to obtain details of protein topology and localization within living cells in a rapid and straightforward manner. To demonstrate the broad applicability of FPP, we used the technique to define the topology of proteins localized to a wide range of organelles including the endoplasmic reticulum (ER), Golgi apparatus, mitochondria, peroxisomes and autophagosomes. The success of the FPP assay in characterizing the topology of the tested proteins within their appropriate compartments suggests this technique has wide applicability in studying protein
Surface expression has attracted much recent interest, and it has been suggested for a variety of applications. Two such applications are whole-cell biocatalysis and the creation of live vaccines. For successful implementation of these applications there is a need for flexible surface expression systems that can yield a high level of expression with a variety of recombinant fusion proteins. The aim of this work was thus to create a surface expression system that would fulfil these requirements.. A novel surface expression system based on the AIDA-I autotransporter was created with the key qualities being are good, protein-independent detection of the expression through the presence of two epitope tags flanking the recombinant protein, and full modularity of the different components of the expression cassette. To evaluate the flexibility of this construct, 8 different model proteins with potential use as live-vaccines or biocatalysts were expressed and their surface expression levels were ...
For proteins in general, its very difficult to cross the cell membrane. The protease will usually digest it, making stability an issue," said lead study author Yunfeng Lu, a UCLA professor of chemical and biomolecular engineering. "Here, weve been able to use this new technology to stabilize the protein, making it very easy to cross the cell membrane, allowing the protein to function properly once inside the cell. This is one of our biggest achievements ...
Grifols to acquire Talecris Biotherapeutics creating a world leading provider of life-saving plasma protein therapies The combination of Grifols and Talecris will create a diversified, global provider of life-saving and life enhancing plasma protein therapeutics built on the strong global presence of Grifols and the established position of Talecris in the United States and Canada. The merger accelerates key strategic initiatives for both Talecris and Grifols as it creates a more efficient platform for manufacturing, innovation and global sales and marketing. Combining the expertise of both companies will build upon their individual legacies of patient commitment, growth and innovation while increasing the availability of high quality plasma protein therapies for patients worldwide. ...
Grifols to acquire Talecris Biotherapeutics creating a world leading provider of life-saving plasma protein therapies The combination of Grifols and Talecris will create a diversified, global provider of life-saving and life enhancing plasma protein therapeutics built on the strong global presence of Grifols and the established position of Talecris in the United States and Canada. The merger accelerates key strategic initiatives for both Talecris and Grifols as it creates a more efficient platform for manufacturing, innovation and global sales and marketing. Combining the expertise of both companies will build upon their individual legacies of patient commitment, growth and innovation while increasing the availability of high quality plasma protein therapies for patients worldwide. ...
Grifols to acquire Talecris Biotherapeutics creating a world leading provider of life-saving plasma protein therapies The combination of Grifols and Talecris will create a diversified, global provider of life-saving and life enhancing plasma protein therapeutics built on the strong global presence of Grifols and the established position of Talecris in the United States and Canada. The merger accelerates key strategic initiatives for both Talecris and Grifols as it creates a more efficient platform for manufacturing, innovation and global sales and marketing. Combining the expertise of both companies will build upon their individual legacies of patient commitment, growth and innovation while increasing the availability of high quality plasma protein therapies for patients worldwide. ...
Grifols to acquire Talecris Biotherapeutics creating a world leading provider of life-saving plasma protein therapies The combination of Grifols and Talecris will create a diversified, global provider of life-saving and life enhancing plasma protein therapeutics built on the strong global presence of Grifols and the established position of Talecris in the United States and Canada. The merger accelerates key strategic initiatives for both Talecris and Grifols as it creates a more efficient platform for manufacturing, innovation and global sales and marketing. Combining the expertise of both companies will build upon their individual legacies of patient commitment, growth and innovation while increasing the availability of high quality plasma protein therapies for patients worldwide. ...
Grifols to acquire Talecris Biotherapeutics creating a world leading provider of life-saving plasma protein therapies The combination of Grifols and Talecris will create a diversified, global provider of life-saving and life enhancing plasma protein therapeutics built on the strong global presence of Grifols and the established position of Talecris in the United States and Canada. The merger accelerates key strategic initiatives for both Talecris and Grifols as it creates a more efficient platform for manufacturing, innovation and global sales and marketing. Combining the expertise of both companies will build upon their individual legacies of patient commitment, growth and innovation while increasing the availability of high quality plasma protein therapies for patients worldwide. ...
DNA sequences comprising nucleic acids encoding fusion proteins comprising an Fc portion of an antibody attached at the N-terminus of an OB protein moiety, vectors comprising such DNA sequences, host cells comprising such vectors or DNA sequences, and processes for preparing such fusion proteins, and pharmaceutical compositions comprising such fusion proteins, are described. The DNA sequences, vectors comprising such DNA sequences, host cells comprising such vectors or DNA sequences, and processes for preparing such fusion proteins, and pharmaceutical compositions comprising such fusion proteins are useful, for example, in providing therapeutically effective amounts of compositions useful for, for example, increasing insulin sensitivity, decreasing the dose of insulin required for the treatment of diabetes, controlling serum glucose levels, increasing lean tissue mass, increasing overall body strength, or regulating bone resorption, or effecting any combination of such, in subjects in need or desirous
A general approach for the sequential labeling of fusion proteins of O(6)-alkylguanine-DNA alkyltransferase (AGT) with different fluorophores in mammalian cells is presented. AGT fusion proteins with different localizations in the cell can be labeled
Anti-LMO1 polyclonal antibody was developed using: Recombinant fusion protein containing a sequence corresponding to amino acids 1-156 of human LMO1 -(NP_002306.1).. This antibody is applicable for use in: Western Blot
We have localized the components of the HOG1 MAP kinase cascade in Saccharomyces cerevisiae. Functional fusions to GFP of the MAPKKK (STE11), the MAPKK (PBS2) and the MAPK (HOG1) allowed all three protein kinases to be localized to the cytoplasm (Figures 1 and 3). Neither STE11 nor PBS2 were observed to undergo altered subcellular localization in stressed cells. In contrast, HOG1-GFP rapidly and reversibly translocated into the nucleus of osmotically stressed cells (Figure 1). These data indicate that activated HOG1 serves to relay the stress signal to the nucleus.. We have defined the minimum cis‐acting requirements for the translocation of HOG1. The phosphorylation of the regulatory threonine and tyrosine residues in the TGY motif of HOG1 is necessary and sufficient for its nuclear translocation. Because a kinase‐impaired mutant of HOG1 still enters the nucleus in stressed cells, HOG1 kinase cannot be directly responsible for activating its own nuclear import. We suggest that ...
BioAssay record AID 683195 submitted by ChEMBL: Agonist activity at human GPR35 expressed in U2OS cells coexpressing Gal4-VP16/beta-arrestin fusion protein after 5 hrs by tango beta-arrestin translocation reporter gene assay.
This control plasmid contains the gene encoding the Cytochrome C oxidase, subunit 8-2 (COX8-2) protein cloned upstream of the SNAP f coding sequence in pSNAP f , as a fusion to the N- terminus of the SNAP-tag
Columbia researchers have discovered how a gene fusion found in 3 percent of glioblastoma tumors boosts mitochondrial activity, triggering cancer. They suggest that a dual-treatment approach, combining a drug that targets the gene fusion protein with a mitochondrial inhibitor, may be effective in slowing the cancers progression.
GenScript Glutathione Resin (L00206) is an affinity chromatography medium designed for easy, one-step purification of recombinant glutathione S-transferase (GST) fusion proteins and other glutathione binding proteins expressed in E. coli, insect cells and mammalian cells.
RTX proteins are composed of a repeating nonamer calcium binding sequence. Often times for repeating protein scaffolds, consensus design is used to create synthetic peptides based on the amino acid frequency at each position. This can lead to higher levels of stability and recombinant expression. The genetic information can also be optimized for easier cloning and concatenation strategies. In exploring consensus design for the RTX protein, we discovered a synthetic sequence that undergoes a reversible phase change in response to calcium binding. We have used this sequence as a non-chromatographic protein purification tag, similar to the elastin like peptide (ELP) tags. By appending the β-roll tag (BRT) to a protein of interest, we can rapidly and efficiently separate the fusion from cell lysate (~ 10 minutes). We have added a protease site between the BRT and protein of interest allowing for the purification of untagged target by precipitation cycling. The image below shows the calcium ...
RTX proteins are composed of a repeating nonamer calcium binding sequence. Often times for repeating protein scaffolds, consensus design is used to create synthetic peptides based on the amino acid frequency at each position. This can lead to higher levels of stability and recombinant expression. The genetic information can also be optimized for easier cloning and concatenation strategies. In exploring consensus design for the RTX protein, we discovered a synthetic sequence that undergoes a reversible phase change in response to calcium binding. We have used this sequence as a non-chromatographic protein purification tag, similar to the elastin like peptide (ELP) tags. By appending the β-roll tag (BRT) to a protein of interest, we can rapidly and efficiently separate the fusion from cell lysate (~ 10 minutes). We have added a protease site between the BRT and protein of interest allowing for the purification of untagged target by precipitation cycling. The image below shows the calcium ...
hardware after fusion - MedHelps hardware after fusion Center for Information, Symptoms, Resources, Treatments and Tools for hardware after fusion. Find hardware after fusion information, treatments for hardware after fusion and hardware after fusion symptoms.
Rent textbook Fusion Protein Technologies for Biopharmaceuticals : Applications and Challenges by Schmidt, Stefan R. - 9780470646274. Price: $184.40
These tools will help advance any experiments utilizing Green Fluorescent Protein or Red Fluorescent Protein fusion constructs.. ...
Pentec Health has been a leading provider of Intradialytic Parenteral Nutrition (IDPN) and Intraperitoneal Nutrition (IPN) protein therapies for malnourished…
Protein Involved In Microtubule-related Processes; GFP-fusion Protein Localizes To The Cytoplasm And Is Induced In Response To The DNA-damaging Agent MMS; YLR412W Is Not An Essential Gene; Similar To Arabidopsis SRR1 Gene
SNAP-tag can be used for labeling proteins inside of cells, on cell surfaces, in solution and on surfaces. ACP-tag is ideal for cell surface labeling as its substrates are non-cell permeable. (In particular, ACP-tag is ideal for labeling subunits of multimeric membrane proteins such as ion channels ...
Unactive, recombinant GST fusion protein containing full-length human p38α/SAPK2a, for use in Kinase Assays. Find MSDS or SDS, a COA, data sheets and more information.
This patent search tool allows you not only to search the PCT database of about 2 million International Applications but also the worldwide patent collections. This search facility features: flexible search syntax; automatic word stemming and relevance ranking; as well as graphical results.
ch3 domain mouse anti human igg ch3 domain | order ch3 domain mouse anti human igg ch3 domain | How to use: ch3 domain mouse anti human igg ch3 domain | support help f
Buy IL35 recombinant protein, IL-35 Recombinant Protein-NP_005746.2 (MBS553262) product datasheet at MyBioSource, Recombinant Proteins
We show that K¿ and K¿ control transfer in every fusion system on a finite p-group when p ¿ 5, and that they control weak closure of elements in every fusion system on a finite p-group when p ¿ 3. This generalizes resultsof ...
We show that K¿ and K¿ control transfer in every fusion system on a finite p-group when p ¿ 5, and that they control weak closure of elements in every fusion system on a finite p-group when p ¿ 3. This generalizes resultsof ...
The equation for the heat of fusion is ?H=n?Hfus, where n is the number of moles and ?Hfus is the molar heat of the substance. Heat of fusion, also known as enthalpy of fusion, is the required...
WebMD provides important information about Vicks Nature Fusion Oral such as if you can you take Vicks Nature Fusion Oral when you are pregnant or nursing or If Vicks Nature Fusion Oral dangerous for children or adults over 60.
The use of the campuss colours works well. Generally, campus colours have been picked by pros to go together. They are a good way to provide a subtle bit of branding that doesnt chew up space. I have no clear idea if there is any reason why some of the bars are in gold and some are in maroon. It seems like the gold might be trying to highlight the main messages, but its a muddied signal (if that is the intention) at best ...
NSF-N, the N-terminal functional domain of the N-ethylmaleimide sensitive fusion protein, consists of two structural domains ...
A protocol for a novel imaging tool for live or fixed mammalian cells that express the HaloTag® protein or protein fusions, for analyzing posttranslational modification of labeled fusion proteins, and isolating proteins and protein complexes.
PubMed Central Canada (PMC Canada) provides free access to a stable and permanent online digital archive of full-text, peer-reviewed health and life sciences research publications. It builds on PubMed Central (PMC), the U.S. National Institutes of Health (NIH) free digital archive of biomedical and life sciences journal literature and is a member of the broader PMC International (PMCI) network of e-repositories.
The present study was undertaken to analyse the capability of HIV-1 derived TAT protein transduction domain (PTD) fused with Green Fluorescent Protein (TAT-GFP) as a delivery vehicle into a range of protozoan parasites. Successful transduction of native purified TAT-GFP was observed by fluorescent microscopy in Cryptosporidium parvum, Giardia duodenalis, and Neospora caninum. The ability to transduce peptides and other cargo into protozoan parasites, will greatly assist in the delivery of future peptide-based drugs and target validation peptides.. ...
Fusarium head blight (FHB) or scab of wheat is a devastating disease in warm and humid regions at wheat-flowering periods worldwide. Natural resistance against FHB pathogens is inadequate and the development of FHB-resistant wheat cultivars has been a challenge. Expression of pathogen-specific antibodies in plants has been proposed as a strategy for crop protection. In this study, an antibody fusion protein comprising a Fusarium-specific recombinant antibody derived from chicken and an antifungal peptide from Aspergillus giganteus was expressed in wheat as a method for protecting plants against FHB pathogens. Plants expressing the antibody fusion displayed a very significantly enhanced resistance in T2 and T3 generations upon single-floret inoculation with the macroconidia of Fusarium asiaticum, the predominant species causing FHB in China, indicating a type II resistance. Spraying inoculation further revealed an enhanced type I resistance in the transgenic wheat plants. Remarkably, more grains ...
Protein transduction domains (PTDs), both naturally occurring and synthetic, have been extensively utilized for intracellular delivery of biologically active molecules both in vitro and in vivo. However, most comparisons of transduction efficiency have been performed using fluorescent markers. To compare efficiency of functional protein transduction, a peptide derived from IkB kinase ß (IKKß) that prevents formation of an active IKK complex was used as a biologically active cargo. This peptide, termed NEMO Binding Domain (NBD), is able to block activation of the transcriptional factor NF-κB by IKK, but not basal NF-κB activity. Our results demonstrate that Antp and Tat PTDs were most effective for delivery of NBD for inhibition of NF-kB activation compared to other PTD-NBD in both Hela and 293 cells, however, at higher concentrations (100 µM), the Antp-NBD as well as the FGF-NBD peptide caused significant cellular toxicity. In contrast to the cell culture results, delivery of NBD using 8K
ANNAPOLIS, Md., Sept. 1, 2011 /PRNewswire/ -- This month, Floridians are recognizing "Plasma Protein Therapies Month," by raising awareness for the valuable contributions of plasma donors throughout the "Sunshine State" and for the rare, genetic diseases treated with the therapies that are made possible through plasma donation.. Plasma protein therapies, which include plasma-derived therapies and recombinant blood clotting factors (a biotechnology product), are used every day to treat people with bleeding disorders, such as hemophilia, that causes painful internal bleeding and debilitating joint damage; primary immunodeficiency diseases, which prevent a person from fighting off even common infections; and alpha-1 antitrypsin deficiency, also known as genetic chronic obstructive pulmonary disease (COPD), a disease that severely damages the liver and lungs. In addition, a plasma protein therapy, albumin, is used in critical care settings, when treating severe trauma, burns and during major ...
Denileukin diftitox has been used for the treatment of a variety of disorders, in particular, malignant lymphoma, another blood-related disease. Denileukin diftitox is believed to be able to specifically attach to and kill malignant mast cells.. Before you can start treatment on this study, you will have what are called screening tests. These tests will help the doctor decide if you are eligible to take part in the study. You will have blood (around 2 teaspoons) and bone marrow samples collected. To collect a bone marrow sample, an area of the hip bone is numbed with anesthetic and a small amount of bone marrow is withdrawn through a large needle. These samples will be used for tests to confirm the diagnosis of the disease. Women who are able to have children must have a negative blood pregnancy test.. If you are found to be eligible, you will receive denileukin diftitox as an injection by vein once a day for 5 days in a row. This will be repeated every 3 weeks (1 cycle). You will receive ...
Proinsulin-transferrin (ProINS-Tf) fusion protein was evaluated for its in vivo pharmacokinetics, efficacy and mechanism. Our previous studies have shown that ProINS-Tf was converted to active insulin (INS)-Tf via the Tf-Tf receptor mediated pathway in hepatoma cells. We hypothesized that this fusion protein can be administered as a prodrug, and be converted to a biologically active protein with specificity for the liver versus other INS-sensitive tissues (muscle and adipose). Administration as an inactive prodrug with liver-specific action compared to other INS-sensitive tissues conceivably reduces negative side-effects seen with other INS analogs. In this report, the data show that ProINS-Tf exhibited a slow, but sustained, in vivo hypoglycemic efficacy and long plasma half-life. The fusion protein showed activity in the liver, as evidenced by decreased expression of two key hepatic glucose production (HGP) enzymes, phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and by increased ...

High Yield Protein Production from Pichia pastoris Yeast: A Protocol for Benchtop Fermentation (         By Julia Cino PhD     ...High Yield Protein Production from Pichia pastoris Yeast: A Protocol for Benchtop Fermentation ( By Julia Cino PhD ...

Protein,Production,from,Pichia,pastoris,Yeast:,A,Protocol,for,Benchtop,Fermentation,biological,advanced biology technology, ... By Julia Cino PhD ... Introduction Over th...The production of a functional protein is intimately related to the ce... Pichia ... Yeast Protein Production System Features High Yields and One-Step Purification. 2. Efficient Cleavage of Fusion Proteins to ... A major use for many of these recombinant organisms is to produce proteins. Since many proteins are of immense commercial value ...
more infohttp://bio-medicine.org/biology-technology/High-Yield-Protein-Production-from-Pichia-pastoris-Yeast-3A-A-Protocol-for-Benchtop-Fermentation-1536-1/

Recombinant Fusion Proteins | Harvard Catalyst Profiles | Harvard CatalystRecombinant Fusion Proteins | Harvard Catalyst Profiles | Harvard Catalyst

"Recombinant Fusion Proteins" by people in Harvard Catalyst Profiles by year, and whether "Recombinant Fusion Proteins" was a ... "Recombinant Fusion Proteins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... Recombinant Fusion Proteins*Recombinant Fusion Proteins. *Proteins, Recombinant Fusion. *Fusion Proteins, Recombinant ... Below are the most recent publications written about "Recombinant Fusion Proteins" by people in Profiles. ...
more infohttps://connects.catalyst.harvard.edu/Profiles/display/Concept/Recombinant%20Fusion%20Proteins

A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in...A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in...

A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in ... A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in ...
more infohttps://www.centerwatch.com/clinical-trials/listings/60439/hemophilia-b-safety-efficacy-extension-study/?geo_lat=32.0852999&geo_lng=34.7817676&radius=10

A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in...A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in...

A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in ... Safety and Efficacy Extension Study of a Recombinant Coagulation Factor IX Albumin Fusion Protein (rIX-FP) in Subjects With ... Coagulation Protein Disorders. Hemorrhagic Disorders. Genetic Diseases, Inborn. Genetic Diseases, X-Linked. ... Subjects who have received FIX products (plasma-derived and / or recombinant FIX) for , 150 exposure days (EDs), confirmed by ...
more infohttps://clinicaltrials.gov/ct2/show/NCT02053792?term=bleeding+episodes&rank=73

Biomolecules | Free Full-Text | Recombinant Fusion Protein Joining E Protein Domain III of Tick-Borne Encephalitis Virus and...Biomolecules | Free Full-Text | Recombinant Fusion Protein Joining E Protein Domain III of Tick-Borne Encephalitis Virus and...

... and characterize a chimeric protein based on the fusion of the bacterial chaperone HSP70 of Yersinia pseudotuberculosis and ... To enhance the immunogenicity of this protein, which has a low molecular weight, the aim of the present work was to express, ... In turn, the incorporation of the HSP70/EIII chimeric protein in the TI-complex resulted in a twofold increase in its ... Using HSP70 in the content of the chimeric protein represents an efficient means for presenting the main antigenic domain of ...
more infohttps://www.mdpi.com/2218-273X/8/3/82

Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a/GNA in Pichia pastoris: sequence...Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a/GNA in Pichia pastoris: sequence...

Production of recombinant protein bio-insecticides on a commercial scale can only be cost effective if host strains with very ... A recombinant fusion protein containing an arthropod toxin, ω-hexatoxin-Hv1a, (from funnel web spider Hadronyche versuta) ... Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a/GNA in Pichia pastoris: sequence ... Introduction of multiple expression cassettes increased the amount of secreted recombinant fusion protein in a laboratory scale ...
more infohttps://link.springer.com/article/10.1007/s10295-014-1466-8?no-access=true

Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells -...Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells -...

In this report, efforts toward the generation of an RSV subunit vaccine using recombinant RSV fusion protein (rRSV-F) are ... The recombinant protein was produced by transient gene expression (TGE) in suspension-adapted human embryonic kidney cells (HEK ... If successful in preclinical and clinical trials, this will be the first recombinant subunit vaccine produced by large-scale ... In this report, efforts toward the generation of an RSV subunit vaccine using recombinant RSV fusion protein (rRSV-F) are ...
more infohttps://infoscience.epfl.ch/record/139485

Mucosal Immunization with Recombinant Fusion Protein DnaJ-ΔA146Ply Enhances Cross-Protective Immunity against Streptococcus...Mucosal Immunization with Recombinant Fusion Protein DnaJ-ΔA146Ply Enhances Cross-Protective Immunity against Streptococcus...

Mucosal Immunization with Recombinant Fusion Protein DnaJ-ΔA146Ply Enhances Cross-Protective Immunity against Streptococcus ... Mucosal Immunization with Recombinant Fusion Protein DnaJ-ΔA146Ply Enhances Cross-Protective Immunity against Streptococcus ... Mucosal Immunization with Recombinant Fusion Protein DnaJ-ΔA146Ply Enhances Cross-Protective Immunity against Streptococcus ... Mucosal Immunization with Recombinant Fusion Protein DnaJ-ΔA146Ply Enhances Cross-Protective Immunity against Streptococcus ...
more infohttps://iai.asm.org/content/82/4/1666/article-info

Cytotoxicity of a recombinant fusion protein of adenovirus early region 4 open reading frame 4 (E4orf4) and human epidermal...Cytotoxicity of a recombinant fusion protein of adenovirus early region 4 open reading frame 4 (E4orf4) and human epidermal...

This study presents an approach for inhibiting p53-deficient tumor cell growth by using protein-based E4orf4 ... protein is a novel cell death factor that selectively induces p53-independent apoptosis in cancer cells, but not in normal ... Cytotoxicity of a recombinant fusion protein of adenovirus early region 4 open reading frame 4 (E4orf4) and human epidermal ... This study presents an approach for inhibiting p53-deficient tumor cell growth by using protein-based E4orf4 that had been ...
more infohttps://insights.ovid.com/pubmed?pmid=16702809

KEX2 Cleavage Regions OF Recombinant Fusion Proteins - Patent applicationKEX2 Cleavage Regions OF Recombinant Fusion Proteins - Patent application

A parental recombinant fusion protein and a test recombinant fusion protein may differ in one, two, three or four amino acids ... 17. The fusion protein encoded by the fusion DNA construct of claim 1. 18. A host cell comprising the fusion DNA construct of ... 12. The fusion DNA construct of claim 1, wherein the desired protein is a therapeutic protein. 13. The fusion DNA construct of ... In some embodiments, the secreted protein is the protein that is released or cleaved from a recombinant fusion polypeptide of ...
more infohttp://www.patentsencyclopedia.com/app/20100055731

Factor IX (Recombinant [Fc Fusion Protein]) | Memorial Sloan Kettering Cancer CenterFactor IX (Recombinant [Fc Fusion Protein]) | Memorial Sloan Kettering Cancer Center

Factor IX (Recombinant [Fc Fusion Protein]) Adult Medication. *. ... Factor IX (Recombinant [Fc Fusion Protein]). ©2018 Memorial ...
more infohttps://www.mskcc.org/cancer-care/patient-education/factor-ix-recombinant-fc-fusion-protein-01

Factor IX (Recombinant), albumin fusion protein Monograph for Professionals - Drugs.comFactor IX (Recombinant), albumin fusion protein Monograph for Professionals - Drugs.com

... albumin fusion protein reference guide for safe and effective use from the American Society of Health-System Pharmacists (AHFS ... Circulating half-life of factor IX (recombinant), albumin fusion protein longer than that of unmodified recombinant or plasma- ... phase I results of recombinant fusion protein linking coagulation factor IX with recombinant albumin (rIX-FP). Thromb Res. 2013 ... Factor IX (Recombinant), albumin fusion protein. Class: Hemostatics. VA Class: BL500. Brands: Idelvion ...
more infohttps://www.drugs.com/monograph/factor-ix-recombinant-albumin-fusion-protein.html

Subject: recombinant fusion proteins / Subject: recombinant fusion proteins - PubAg Search ResultsSubject: 'recombinant fusion proteins' / Subject: recombinant fusion proteins - PubAg Search Results

... recombinant fusion proteins Subject recombinant fusion proteins Remove constraint Subject: recombinant fusion proteins Start ... at 10 weeks of age with recombinant LHRH fusion proteins were investigated. Recombinant fusion proteins, ovalbumin-LHRH-7 and ... recombinant fusion proteins, etc ; Glycine max; soybeans; grain crops; embryo (plant); plant proteins; proline; protein ... the phage protein III lacks its indigenous signal peptide required for protein secretion, thus recombinant fusion proteins are ...
more infohttps://pubag.nal.usda.gov/?f%5Bsubject_term%5D%5B%5D=recombinant+fusion+proteins&page=1&q=%22recombinant+fusion+proteins%22&search_field=subject&sort=date-asc

Subject: recombinant fusion proteins / Journal: Plant & cell physiology - PubAg Search ResultsSubject: 'recombinant fusion proteins' / Journal: Plant & cell physiology - PubAg Search Results

You searched for: Subject recombinant fusion proteins Remove constraint Subject: recombinant fusion proteins Journal Plant ... recombinant fusion proteins, etc ; Triticum aestivum; wheat; plasma membrane; plant proteins; membrane proteins; malic acid; ... recombinant fusion proteins, etc ; Arabidopsis thaliana; meristems; plant proteins; calcium-binding proteins; complementary DNA ... recombinant fusion proteins, etc ; Zea mays; corn; Zoysia japonica; C4 plants; bundle sheath cells; plant proteins; malic ...
more infohttps://pubag.nal.usda.gov/?f%5Bjournal_name%5D%5B%5D=Plant+%26+cell+physiology&q=%22recombinant+fusion+proteins%22&search_field=subject&sort=title

Factor Ix Fc Fusion Protein Recombinant (Intravenous Route) Description and Brand Names - Mayo ClinicFactor Ix Fc Fusion Protein Recombinant (Intravenous Route) Description and Brand Names - Mayo Clinic

Factor IX Fc fusion protein recombinant injection is used as an on-demand treatment to control or prevent bleeding episodes, ... Factor IX is a protein that is produced naturally in the body. Alprolix® is a man-made protein produced to replicate the ...
more infohttps://www.mayoclinic.org/drugs-supplements/factor-ix-fc-fusion-protein-recombinant-intravenous-route/description/drg-20095291

Eloctate (Antihemophilic Factor (Recombinant), Fc Fusion Protein for Intravenous Infusion): Side Effects, Interactions, Warning...Eloctate (Antihemophilic Factor (Recombinant), Fc Fusion Protein for Intravenous Infusion): Side Effects, Interactions, Warning...

Fc Fusion Protein for Intravenous Infusion) may treat, uses, dosage, side effects, drug interactions, warnings, patient ... Fc Fusion Protein] for Intravenous Injection. DESCRIPTION. ELOCTATE, Antihemophilic Factor (Recombinant), Fc Fusion Protein, is ... ELOCTATE, Antihemophilic Factor (Recombinant), Fc Fusion Protein, is a recombinant DNA derived, antihemophilic factor indicated ... Fc fusion protein (BDD-rFVIIIFc) is the active ingredient in ELOCTATE. BDD-rFVIIIFc is a recombinant protein consisting of a B- ...
more infohttps://www.rxlist.com/eloctate-drug.htm

WO1998050432 RECOMBINANT ANTIBODY-ENZYME FUSION PROTEINSWO1998050432 RECOMBINANT ANTIBODY-ENZYME FUSION PROTEINS

The invention relates to recombinantly produced fusion polypeptides comprising antibody V¿H? and V¿L? sequences operatively ...
more infohttps://patentscope.wipo.int/search/en/detail.jsf?docId=WO1998050432&tab=PCTDOCUMENTS

Frontiers | A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts...Frontiers | A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts...

The recombinant fusion proteins F1-LcrV and F1-LcrV-HSP70(II) were purified using Ni-NTA columns and formulated with alum to ... The recombinant fusion proteins F1-LcrV and F1-LcrV-HSP70(II) were purified using Ni-NTA columns and formulated with alum to ... Both the recombinant constructs caf1-lcrV and caf1-lcrV-hsp70(II) were cloned in pET28a vector and expressed in Escherichia ... Both the recombinant constructs caf1-lcrV and caf1-lcrV-hsp70(II) were cloned in pET28a vector and expressed in Escherichia ...
more infohttps://www.frontiersin.org/articles/10.3389/fmicb.2016.01053/full

Eloctate (antihemophilic factor (recombinant), fc fusion protein) dose, indications, adverse effects, interactions... from PDR...Eloctate (antihemophilic factor (recombinant), fc fusion protein) dose, indications, adverse effects, interactions... from PDR...

Antihemophilic factor Fc fusion protein is a fully recombinant, fusion protein that temporarily replaces the missing ... Recombinant, fusion protein with antihemophilic factor linked to the Fc protein fragment of human IgG1. Used for the control ... Fc fusion protein and any potential adverse effects on the breast-fed infant from antihemophilic factor, Fc fusion protein or ... Fc fusion protein and any potential adverse effects on the breast-fed infant from antihemophilic factor, Fc fusion protein or ...
more infohttps://www.pdr.net/drug-summary/Eloctate-antihemophilic-factor--recombinant---fc-fusion-protein-3581

Factor ix albumin fusion protein recombinant (By injection) | Drug Notes | Health Information | St. Lukes HospitalFactor ix albumin fusion protein recombinant (By injection) | Drug Notes | Health Information | St. Luke's Hospital

Factor ix albumin fusion protein recombinant (By injection). Factor IX Albumin Fusion Protein Recombinant (FAK-tor NINE al-BUE- ... You should not receive it if you had an allergic reaction to factor IX albumin fusion protein recombinant or hamster proteins. ...
more infohttps://www.stlukes-stl.com/health-content/drug-notes/45/6181.htm

Recombinant human ADRB2 + GsaL fusion protein (ab90837)Recombinant human ADRB2 + GsaL fusion protein (ab90837)

GsaL fusion protein. Ab90837 is an active full length protein produced in Baculovirus infected Sf9 cells and has been… ... Recombinant human ADRB2 + GsaL fusion protein. See all ADRB2 + GsαL fusion proteins and peptides. ... Guanine nucleotide binding protein (G protein) alpha stimulating activity polypeptide 1. *Guanine nucleotide binding protein G( ... This fusion protein contains a thrombin cleavage site (TS) between the His tag and GsaL subunit. ...
more infohttp://www.abcam.com/recombinant-human-adrb2-gsalphal-fusion-protein-ab90837.html

Modern Care Journal | Can Multi-Stage Recombinant Fusion Proteins be Considered as Reliable Vaccines Against Tuberculosis? A...Modern Care Journal | Can Multi-Stage Recombinant Fusion Proteins be Considered as Reliable Vaccines Against Tuberculosis? A...

Can Multi-Stage Recombinant Fusion Proteins be Considered as Reliable Vaccines Against Tuberculosis? A Letter to the Editor ... To Cite: Keikha M, Karbalaei M. Can Multi-Stage Recombinant Fusion Proteins be Considered as Reliable Vaccines Against ... multi-stage fusion peptides, viral vector vaccines, DNA vaccines, and protein subunit vaccines. Overall, TB candidate vaccines ... a recombinant influenza virus H1N1 with two main antigens of Mtb, ESAT-6 and Ag85B), and Ad5Ag85A (a recombinant non- ...
more infohttp://mcjbums.com/en/articles/91493.html

Recombinant fusion protein of Heparin-Binding Hemagglutinin Adhesin and Fibronectin Attachment Protein (rHBHA-FAP) of...Recombinant fusion protein of Heparin-Binding Hemagglutinin Adhesin and Fibronectin Attachment Protein (rHBHA-FAP) of...

Based on MAP pathogenesis, it seems that research about the production of new recombinant proteins to stimulate cell-mediated ... This study describes successful expression and purification of a chimeric fusion protein which consists of Heparin-Binding ... Triggered antigen-specific IFN-γ response of isolated PBMCs from immunized goats to rHBHA-FAP and all crude proteins of MAP ( ... stimulated by constructed chimeric protein from rHBHA-FAP and PPD vaccinated goats. Antigen-specific gamma interferon (IFN-γ) ...
more infohttps://gutpathogens.biomedcentral.com/articles/10.1186/s13099-019-0317-6

SNU Open Repository and Archive: Genetic engineering and expression of a recombinant fusion protein processing basic fibroblast...SNU Open Repository and Archive: Genetic engineering and expression of a recombinant fusion protein processing basic fibroblast...

Genetic engineering and expression of a recombinant fusion protein processing basic fibroblast growth factor and fibronectin ...
more infohttp://s-space.snu.ac.kr/handle/10371/24594
  • Modeling and Simulation of Production of Metallothionein and Red Fluorescent Fusion Protein by Recombinant Escherichia Coli Using Graphical Programming, Modeling, Programming and Simulations Using LabVIEW™ Software Riccardo De Asmundis, IntechOpen, DOI: 10.5772/14091. (intechopen.com)
  • To enhance the immunogenicity of this protein, which has a low molecular weight, the aim of the present work was to express, isolate, and characterize a chimeric protein based on the fusion of the bacterial chaperone HSP70 of Yersinia pseudotuberculosis and EIII (DIII + stem) as a prospective antigen for an adjuvanted delivery system, the tubular immunostimulating complex (TI-complex). (mdpi.com)
  • The resulting plasmid was transformed into DE3 cells for the heterologous expression of the chimeric protein, which was purified by immobilized metal affinity chromatography (IMAC). (mdpi.com)
  • ELISA, differential scanning calorimetry, intrinsic fluorescence, and computational analysis were applied for the characterization of the immunogenicity and conformation of the chimeric protein. (mdpi.com)
  • Mice immunization showed that the chimeric protein induced twice the number of anti-EIII antibodies in comparison with EIII alone. (mdpi.com)
  • In turn, the incorporation of the HSP70/EIII chimeric protein in the TI-complex resulted in a twofold increase in its immunogenicity. (mdpi.com)
  • The formation of this vaccine construction was accompanied by significant conformational changes in the chimeric protein. (mdpi.com)
  • Using HSP70 in the content of the chimeric protein represents an efficient means for presenting the main antigenic domain of the TBEV envelope protein to the immune system, whereas the incorporation of this chimeric protein into the TI-complex further contributes to the development of a stronger immune response against the TBEV infection. (mdpi.com)
  • Significant increases were observed in the IFN-γ production level of peripheral blood mononuclear cells (PBMCs) stimulated by constructed chimeric protein from rHBHA-FAP and PPD vaccinated goats. (biomedcentral.com)
  • Antigen-specific gamma interferon (IFN-γ) secretion in positive group (immunized by PPD) against rHBHA-FAP and test group (immunized by rHBHA-FAP) against PPD, also statistically insignificant rises between stimulation with rHBHA-FAP and PPD, suggested the potential and specificity of our chimeric protein to stimulate cell mediated immunity against MAP. (biomedcentral.com)
  • These modifications did not affect the insecticidal activity of the recombinant toxin towards lepidopteran larvae. (springer.com)
  • Fitches EC, Bell HA, Powell ME, Back E, Sargiotti C, Weaver RJ, Gatehouse JA (2010) Insecticidal activity of scorpion toxin (ButaIT) and snowdrop lectin (GNA) containing fusion proteins towards pest species of different orders. (springer.com)
  • Fitches EC, Edwards MG, Mee C, Grishin E, Gatehouse AMR, Edwards JP, Gatehouse JA (2004) Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion. (springer.com)
  • The affinity, as well as association and dissociation rates of the complex, was measured for human and bovine protein S at five different calcium concentrations. (usda.gov)
  • To investigate the mechanism of phytochrome action in vivo, NtPHYB, AtPHYB and phyD:green fluorescent protein (GFP) were overexpressed in Nicotiana plumbaginifolia and Arabidopsis thaliana. (usda.gov)
  • Domain III (DIII) of the tick-borne encephalitis virus (TBEV) protein E contains epitopes, which induce antibodies capable of neutralizing the virus. (mdpi.com)
  • Attention has been given to epitopes from the hemagglutinin (HA) stem region in order to raise neutralizing antibodies against conserved structures of the protein ( 2 - 6 ). (frontiersin.org)
  • Recombinant factor VIII Fc fusion protein: extended-interval dosing maintains low bleeding rates and correlates with von Willebrand factor levels. (eloctate.com)
  • Just as the blades of a windmill harness naturally occurring wind to produce energy, Fc Fusion utilizes naturally occurring Fc receptors in your body to keep Factor VIII temporarily recirculating in your bloodstream, protecting you from bleeds. (eloctate.com)
  • The recombinant protein was produced by transient gene expression (TGE) in suspension-adapted human embryonic kidney cells (HEK-293E) in 4L orbitally shaken bioreactors. (epfl.ch)
  • The recombinant fusion proteins F1-LcrV and F1-LcrV-HSP70(II) were purified using Ni-NTA columns and formulated with alum to evaluate the humoral and cell mediated immune responses in mice. (frontiersin.org)
  • Most importantly, immune responses to NPLs that also contained recombinant hemagglutinin (HA) were strongly enhanced in a CTA1-enzyme dependent manner and we achieved broadly protective immunity against a lethal infection with heterosubtypic influenza virus. (frontiersin.org)
  • Recombinant Fusion Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • The interaction between vitamin K-dependent protein S and the C4b-binding protein (C4BP) was studied using surface plasmon resonance and genetic engineering. (usda.gov)
  • This graph shows the total number of publications written about "Recombinant Fusion Proteins" by people in Harvard Catalyst Profiles by year, and whether "Recombinant Fusion Proteins" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Recombinant Fusion Proteins" by people in Profiles. (harvard.edu)
  • Fitches EC, Pyati PS, King GF, Gatehouse JA (2012) Fusion to snowdrop lectin dramatically enhances the oral activity of the insecticidal peptide ω-hexatoxin-Hv1a by mediating its delivery to the central nervous system. (springer.com)