Recombinant Fusion Proteins
Molecular Sequence Data
Amino Acid Sequence
Cloning, Molecular
Escherichia coli
Base Sequence
Vaccines, Synthetic
Immunotoxins
Membrane Fusion
Viral Fusion Proteins
Cell Fusion
Genetic Vectors
DNA, Complementary
Immunoconjugates
Protein Binding
Sequence Homology, Amino Acid
Glutathione Transferase
Enzyme-Linked Immunosorbent Assay
Gene Expression
Plasmids
DNA Primers
Blotting, Western
Binding Sites
Immunoblotting
Electrophoresis, Polyacrylamide Gel
Antibody Specificity
Immunoglobulin G
Sequence Alignment
Diphtheria Toxin
Tumor Cells, Cultured
Polymerase Chain Reaction
Autoantibodies
Oncogene Proteins, Fusion
Rabbits
Cattle
Gene Fusion
Spinal Fusion
T-Lymphocytes
ADP Ribose Transferases
Protein Structure, Tertiary
Transfection
DNA, Recombinant
Green Fluorescent Proteins
Peptide Fragments
Cells, Cultured
Luminescent Proteins
Bacterial Toxins
Mutation
Cricetinae
Maltose-Binding Proteins
Membrane Proteins
Baculoviridae
Viral Envelope Proteins
beta-Galactosidase
Recombination, Genetic
Carrier Proteins
Cercopithecus aethiops
Oncogene Fusion
Mutagenesis, Site-Directed
Protein Engineering
CHO Cells
Cell Membrane
HeLa Cells
Spodoptera
DNA-Binding Proteins
Transcription Factors
COS Cells
Peptides
Virus Internalization
Transcription, Genetic
Protein Conformation
RNA, Messenger
Immunoglobulin Fc Fragments
Restriction Mapping
Substrate Specificity
Saccharomyces cerevisiae
Translocation, Genetic
Pichia
Microscopy, Fluorescence
DNA
Vesicular Transport Proteins
Promoter Regions, Genetic
Models, Molecular
Protein Transport
Giant Cells
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)https://www.medicinenet.com › Medical Dictionary › G
A genetic translocation is a change in the number or arrangement of the chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material, which can have significant effects on the individual.
Genetic Translocation | Definition & Facts | Britannica
https://www.britannica.com › science › Genetic-tr...
Genetic translocation, also called chromosomal translocation, a type of chromosomal aberration in which a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material. Genetic translocations are often found in cancer cells and may play a role in the development and progression of cancer.
Translocation, Genetic | health Encyclopedia - UPMC
https://www.upmc.com › health-library › gene...
A genetic translocation is a change in the number or arrangement of the chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material, which can have significant effects on the individual.
Genetic Translocation | Genetics Home Reference - NIH
https://ghr.nlm.nih.gov › condition › ge...
A genetic translocation is a change in the number or arrangement of the chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome. This can result in a gain or loss of genetic material, which can have significant effects on the individual.
In conclusion, Genetic Translocation is an abnormality in the number or arrangement of chromosomes in a cell. It occurs when a portion of one chromosome breaks off and attaches to another chromosome, resulting in a gain or loss of genetic material that can have significant effects on the individual.
Factor IX
PLGLB2
Efmoroctocog alfa
Moxetumomab pasudotox
Etanercept
TROVE2
Regulatory macrophages
TopoTarget
Zearalenone
HaloTag
FLAG-tag
Protein tag
COVID-19 vaccine clinical research
Immunotoxin
TEV protease
Fusion protein
Atacicept
Cancer vaccine targeting CD4+ T cells
NGR-hTNF (antitumor recombinant protein)
Sporosarcina ureae
Nuclear-inclusion-a endopeptidase
CD4 immunoadhesin
DHX8
Biological therapy for inflammatory bowel disease
Sanofi
Thomas Schuler
Beta thalassemia
Bone morphogenetic protein 2
Human metapneumovirus
Albinterferon
Phage display
Pal Maliga
NE-tag
Toxin
Index of biochemistry articles
Orthohantavirus
Belimumab
Haloferax volcanii
EGTA (chemical)
Cathepsin F
Behavioral neuroscience
Transgene
Influenza
Pestivirus
Retinaldehyde-binding protein 1
Filoviridae
Endothelial cell tropism
Feline coronavirus
Recombinant AAV mediated genome engineering
Nirsevimab
Garry Nolan
Oncolytic virus
Sir William Dunn School of Pathology
GCS1
Glossary of virology
Tumor antigens recognized by T lymphocytes
Alfred G. Gilman
Biopharmaceutical
111In-Labeled recombinant gelonin toxin-B lymphocyte stimulator protein fusion protein - PubMed
Antihemophilic Factor (Recombinant [Fc-VWF-XTEN Fusion Protein]: Pediatric Medication | Memorial Sloan Kettering Cancer Center
A designed recombinant fusion protein for targeted delivery of siRNA to the mouse brain - PubMed
ELOCTATE® [Antihemophilic Factor (Recombinant), FC Fusion Protein] Financial Assistance Programs - Sanofi U.S.
Utility of recombinant fusion protein ESAT6-CFP10 skin test for differential diagnosis of active tuberculosis: A prospective...
Recombinant Fusion Proteins | Anatomical Neuropharmacology Unit
ALPROLIX® [Coagulation Factor IX (Recombinant), Fc Fusion Protein]
Activation of Recombinant Diphtheria Toxin Fusion Proteins by Specific Proteases Highly Expressed on the Surface of Tumor Cells...
Androstane metabolites bind to and deactivate the nuclear receptor CAR-beta
Aflibercept - Drugs and Lactation Database (LactMed®) - NCBI Bookshelf
DeCS 2006 - Deleted terms
These highlights do not include all the information needed to use ALTUVIIIO safely and effectively. See full prescribing...
Biodistribution, pharmacokinetics, and nuclear imaging studies of 111In-labeled rGel/BLyS fusion toxin in SCID mice bearing B...
Recombinant Mycobacterium bovis bacillus Calmette-Guérin expressing Ag85B-IL-7 fusion protein enhances IL-17A-producing innate...
Retroviral vectors displaying functional antibody fragments - PubMed
Publication Detail
APG101 in Glioblastoma - Full Text View - ClinicalTrials.gov
Hemophilia A (Factor VIII Deficiency): Practice Essentials, Background, Pathophysiology
AbMiner - Antibody Detail | Genomics and Pharmacology Facility
Biomarkers Search
Vaccination for Hepatitis C Virus: An Evasive Target
Irmgard Behlau, M.D. | Harvard Catalyst Profiles | Harvard Catalyst
Delta Variant RBD protein | Luciferase tagged | InvivoGen
CanMED: NDC
An extra dimension in protein tagging by quantifying universal proteotypic peptides using targeted proteomics | Scientific...
EMEA-001793-PIP01-15-M03 | European Medicines Agency
長岡 正人 (Masato Nagaoka) - マイポータル - researchmap
NIOSHTIC-2 Search Results - Full View
Antibody9
- We fused the gene encoding an antibody fragment directed against a hapten with that encoding the viral envelope protein (Pr80env) of the ecotropic Moloney murine leukemia virus. (nih.gov)
- Furthermore the hapten-binding particles were able to transfer the neo gene and the antibody-envelope fusion gene to mouse fibroblasts. (nih.gov)
- In principle, the display of antibody fragments on the surface of recombinant retroviral particles could be used to target virus to cells for gene delivery, or to retain the virus in target tissues. (nih.gov)
- APG101 is a fusion protein (similar to an antibody) and will be administered as a weekly infusion. (clinicaltrials.gov)
- 15. Antibody fusion proteins: anti-CD22 recombinant immunotoxin moxetumomab pasudotox. (nih.gov)
- Recombinant protein vaccines that induce anti-envelope antibody responses are unlikely to provide sterilizing immunity owing to the genetic variability of the HCV envelope region - but may yet play a role in attenuating the course of primary infection or serve as an adjunct to a T-cell-based vaccine. (medscape.com)
- Protein levels can be obtained by antibody-based approaches such as classical enzyme-linked immunosorbent assays (ELISA) experiments with theoretical detection and quantification limits in the zeptomolar concentration range 7 . (nature.com)
- Antibody recognition of the mutant proteins was determined by inhibition ELISA. (cdc.gov)
- The NIAID Laboratory of Malaria Immunology and Vaccinology (LMIV), Vaccine Development Unit, has an open position for a malaria vaccine staff scientist to lead LMIV's Recombinant Antigen and Antibody Development Unit. (nih.gov)
Peptides3
- In this work, we describe the selection of peptides with ideal mass spectrometry characteristics for use in quantification of tagged proteins using targeted proteomics. (nature.com)
- We mined the proteome of the hyperthermophile Pyrococcus furiosus to obtain two peptides that are unique in the proteomes of all known model organisms (proteotypic) and allow sensitive quantification of target proteins in a complex background. (nature.com)
- By combining these 'Proteotypic peptides for Quantification by SRM' (PQS peptides) with epitope tags, we demonstrate their use in co-immunoprecipitation experiments upon transfection of protein pairs, or after introduction of these tags in the endogenous proteins through genome engineering. (nature.com)
Targeting peptide1
- The designed fusion protein designated as TARBP-BTP consists of a double-stranded RNA-binding domain (dsRBD) of human Trans Activation response element (TAR) RNA Binding Protein (TARBP2) fused to a brain targeting peptide that binds to monosialoganglioside GM1. (nih.gov)
Nucleocapsid proteins2
- LIPS method for the detection of SARS-CoV-2 antibodies to spike and nucleocapsid proteins. (invivogen.com)
- A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins. (nih.gov)
Purification3
- 6. Expression, purification, and immobilization of recombinant tamavidin 2 fusion proteins. (nih.gov)
- 7. Tamavidin, a versatile affinity tag for protein purification and immobilization. (nih.gov)
- They enable the detection of the protein in the cell and allow the purification of the associated protein complex. (nature.com)
Mycobacterium1
- We here constructed a recombinant Mycobacterium bovis bacillus Calmette-Guérin expressing antigen 85B (Ag85B)-IL-7 fusion protein (rBCG-Ag85B-IL-7). (elsevierpure.com)
Monoclonal1
- Luciferase-tagged RBD proteins are ideal for studying the binding of anti-spike monoclonal antibodies (mAbs) by solid-phase ELISA and/or solution‑phase LIPS assays, as well as anti‑spike polyclonal antibodies in the sera of recovered COVID‑19 patients and/or vaccinees by LIPS [1-3]. (invivogen.com)
Endogenous5
- The endogenous use of these tags for detailed protein characterization is widespread in lower organisms that allow for efficient homologous recombination. (nature.com)
- With the recent advances in genome engineering, tagging of endogenous proteins is now within reach for most experimental systems, including mammalian cell lines cultures. (nature.com)
- Endogenous protein tagging for absolute quantification provides a powerful extra dimension to protein analysis, allowing the detailed characterization of endogenous proteins. (nature.com)
- In rat and mouse fibroblasts, green fluorescent protein chimera and endogenous RhoG proteins colocalize according to a tubular cytoplasmic pattern, with perinuclear accumulation and local concentration at the plasma membrane. (cnrs.fr)
- RhoG-dependent events are not mediated through a direct interaction with Rac1 and Cdc42Hs targets such as PAK-1, POR1, or WASP proteins but require endogenous Rac1 and Cdc42Hs activities: coexpression of a dominant negative Rac1 impairs membrane ruffling and lamellipodia but not filopodia or microvilli formation. (cnrs.fr)
Complexes3
- The use of protein tagging to facilitate detailed characterization of target proteins has not only revolutionized cell biology, but also enabled biochemical analysis through efficient recovery of the protein complexes wherein the tagged proteins reside. (nature.com)
- The incumbent will work in a NIAID laboratory that designs and tests malaria vaccine candidates for transmission blocking and pregnancy malaria using biochemistry, immunology, and microbiology tools to examine proteins, protein complexes, fusion proteins, and preclinical model responses. (nih.gov)
- Characterization of DNA-protein complexes by nanoparticle tracking analysis and their association with systemic lupus erythematosus. (nih.gov)
Characterization2
Human4
- Antibodies to ribosomal P2 protein were rarely detected, ransmission routes of human parvovirus 4 (PARV4), except in patients with systemic lupus erythematosus ( 5 ). (cdc.gov)
- 20. Burkavidin: a novel secreted biotin-binding protein from the human pathogen Burkholderia pseudomallei. (nih.gov)
- Recombinant fusion protein of human ACP1 (NP_009030.1). (antikoerper-online.de)
- Recombinant fusion protein containing a sequence corresponding to amino acids 1-132 of human RPS12 (NP_001007.2). (fishersci.com)
Ribosomal1
- The control protein was ribosomal P2 protein fused to SUMO. (cdc.gov)
Molecule1
- Aflibercept is a large protein molecule with a molecular weight of 115,000, absorption is unlikely because it is probably partly destroyed in the infant's gastrointestinal tract and poorly absorbed orally, so systemic effects in infants are not expected. (nih.gov)
Mutant3
- 9. Recombinant NeutraLite avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific binding properties. (nih.gov)
- Inhibition ELISA with the mutant proteins indicated that epitope 126-131 was the dominant epitope, but mutation of epitope 120-125 was also required to eliminate mAb reactivity to Hev b 5. (cdc.gov)
- We have expressed mutant RhoG proteins fused to the green fluorescent protein and analyzed subsequent changes in cell surface morphology and modifications of cytoskeletal structures. (cnrs.fr)
Affinity1
- RBD‑LuciaV8 (B.1.617.2) has been generated by recombinant DNA technology, produced in CHO cells, and purified by IMAC (Immobilized Metal Affinity Chromatography) using a C‑terminal histidine tag. (invivogen.com)
Antibodies1
- The antibodies did not appear to recognize the epitope 63-68 in the recombinant fusion protein. (cdc.gov)
Expression1
- Expression of chimeric envelope proteins in helper cell lines and integration into Moloney murine leukemia virus particles. (nih.gov)
Genes1
- 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. (nih.gov)
Cells7
- Because of its specificity of binding to B cells, BLyS-derived fusion toxins such as the gelonin (Gel)-BLyS fusion protein has been studied by investigators to selectively target and treat B cell malignancies (3-6). (nih.gov)
- However, mammalian cells can internalize the toxin in association with a carrier, at which point Gel is lethal to the cells because it inhibits protein synthesis completely within 3-4 days of internalization and release within the cell. (nih.gov)
- therefore, these fusion proteins bind preferentially to these cancer cells. (nih.gov)
- The fusion gene was co-expressed in ecotropic retroviral packaging cells with a retroviral plasmid carrying the neomycin phosphotransferase gene (neo), and retroviral particles with specific hapten binding activities were recovered. (nih.gov)
- Daybue is a twice daily oral solution that works by reducing inflammation in the brain, stopping certain types of cells from becoming overactive, and increasing the amount of the naturally occurring protein called IGF-1. (primetherapeutics.com)
- They promote cell membrane fusion and thereby may function in the uptake of the virus by cells. (nih.gov)
- Microtubule depolymerization upon nocodazole treatment leads to a loss of RhoG protein from the cell periphery associated with a reversal of the RhoG phenotype, whereas PDGF or bradykinin stimulation of nocodazole-treated cells could still promote Rac1- and Cdc42Hs-dependent cytoskeletal reorganization. (cnrs.fr)
Vaccine1
- Recombinant protein hepatitis C vaccine studies. (medscape.com)
Epitope1
- Site-directed mutagenesis was used to selectively eliminate the IgG binding for each epitope and single and multiple mutations were expressed as recombinant GST fusion proteins. (cdc.gov)
Viral protein1
- They were named viral protein (VP) 2 and in Taiwan, we detected DNA in plasma of 3 mothers and their newborns with hydrops. (cdc.gov)
Gene1
- The protein encoded by this gene is similar to the protein transgelin, which is one of the earliest markers of differentiated smooth muscle. (caslab.com)
Detection1
- 17. Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation. (nih.gov)
Small1
- 272-630 and aa 604-914 of ORF2, were fused to bacterial and Chien-Ching Hung small ubiquitin-like modifi er (SUMO) protein (a member of a ubiquitin-like protein family) and used as antigens in In studying the epidemiology of parvovirus 4 (PARV4) immunoblot. (cdc.gov)
Active2
- Utility of recombinant fusion protein ESAT6-CFP10 skin test for differential diagnosis of active tuberculosis: A prospective study. (bvsalud.org)
- Constitutively active RhoG proteins produce morphological and cytoskeletal changes similar to those elicited by a simultaneous activation of Rac1 and Cdc42Hs, i.e., the formation of ruffles, lamellipodia, filopodia, and partial loss of stress fibers. (cnrs.fr)
Cell2
- This invention relates to diphtheria toxin fusion proteins comprising a diphtheria toxin (DT) cell-killing component and a cell-binding component such as granulocyte macrophage colony-stimulating factor (GM-CSF), interleukin 2 (IL-2), or epidermal growth factor (EGF). (nih.gov)
- 5. Phase I trial of anti-CD22 recombinant immunotoxin moxetumomab pasudotox (CAT-8015 or HA22) in patients with hairy cell leukemia. (nih.gov)
Tags1
- However, none of these tags allow for a direct quantification of the protein. (nature.com)
Structure1
- Plasticity in structure and assembly of SARS-CoV-2 nucleocapsid protein. (nih.gov)