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
The demand of monospecific high affinity binding reagents, particularly monoclonal antibodies, has been steadily increasing over the last years. Enhanced throughput of antibody generation has been addressed by optimizing in vitro selection using phage display which moved the major bottleneck to the production and purification of recombinant antibodies in an end-user friendly format. Single chain (sc)Fv antibody fragments require additional tags for detection and are not as suitable as immunoglobulins (Ig)G in many immunoassays. In contrast, the bivalent scFv-Fc antibody format shares many properties with IgG and has a very high application compatibility. In this study transient expression of scFv-Fc antibodies in human embryonic kidney (HEK) 293 cells was optimized. Production levels of 10-20 mg/L scFv-Fc antibody were achieved in adherent HEK293T cells. Employment of HEK293-6E suspension cells expressing a truncated variant of the Epstein Barr virus (EBV) nuclear antigen (EBNA) 1 in combination with
Abstract: Allergic responses are strongly associated with Th2-type immune responses, and modulation of the skewed Th2 response toward a more balanced response is the major goal of allergen immunotherapy (IT) in allergic disorders. To achieve this goal, several approaches have been tested. The authors previously showed that a human immunoglobulin (Ig) Fcg-Fce fusion protein (GE2) that directly cross-links FceRI and FcgRIIb on human mast cells and basophils was able to inhibit degranulation, and they reasoned that human gamma-allergen fusion protein would achieve a similar inhibitory effect in an allergen-specific fashion while preserving the immunogenicity of the allergen component. Therefore, the authors constructed and developed a human-cat chimeric fusion protein composed of the human Fcg1 and the cat allergen Fel d1 (Felis domesticus) for cat allergen-specific IT. This article summarizes the therapeutic features and potential of this novel fusion protein for allergic IT.. Chimeric human ...
Phase I study of bintrafusp alfa, a bifunctional fusion protein targeting TGF-β and PD-L1, in patients with pretreated biliary tract cancer ...
The goals of this study were to build a yeast platform for the secretion of a variety of scFv/scTCR GFP fusion proteins and to understand the effects that fusion protein construction can have on intracellular fusion protein processing. A large collection of 27 GFP fusion proteins having scFv/scTCR fusion partners representative of a wide range of secretion fitnesses was analyzed. It was discovered that the fusion secretion levels were governed by scFv/scTCR secretion fitness, rather than by GFP, linker length, or fusion orientation. In addition, type III fusions were the most fluorescent with the least amount of observed degradation, and therefore, they represent the recommended construct for secretion of GFP fusions from yeast. Finally, fusion to GFP clearly affected the intracellular processing of the scFv/scTCR, and in particular helped promote the exit of mature protein from the cell. Finally, large amounts of fully active fusion protein accumulated inside the cell as a result of secretory ...
Sandwich, UK -- Levicept Ltd., an asset-centric biotechnology company focused on the development of LEVI-04, a first-in-class treatment for chronic pain indications,…
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.
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 ...
RATIONALE: DTGM fusion protein may be able to locate cancer cells and stop them from growing. PURPOSE: Phase I/II trial to study the effectivenes
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 ...
SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that are commonly comprised of four structural proteins: Spike protein(S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1). SARS-CoV-2 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2 (2). In SARS-Cov-2, as with most coronaviruses, proteolytic cleavage of the S protein into two distinct peptides, S1 and S2 subunits, is required for activation. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (3-5). Based on structural biology studies, the receptor binding domain (RBD), located in the C-terminal region of S1, can be oriented either in the up/standing or down/lying state (6). The standing state is associated with higher ...
We describe here a simple method for expression, extraction, and purification of recombinant human IgG fused to GFP in Nicotiana...
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 ...
HHUMath.-Nat. FakultätBiologieMikrobiologieMehrUstilago communityTypes of genetic engeneering5.8 C-terminal fusion with TapTag (ctt; fusion) ...
Rat CD40 / TNFRSF5 protein (8229-CD) is manufactured by R&D Systems, over 95% purity. Reproducible results in bioactivity assays. Learn More...
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. ...
Introduction SNAP-Tag fusion proteins can be expressed by transient or by stable transfection. For expression of fusion proteins with the SNAP-Tag refer to instructions supplied with the SNAP-Tag plasmids
Dendritic cells (DCs) are critical in the process of inducing immunity and peripheral tolerance. This fact opened the possibility that these cells may be targets of possible manipulations aimed at producing immunotherapeutic inducers or suppressors of the immune response. Recently it was shown that antigens can be sent directly to the DCs (Hawiger et al. 2001; Bonifaz et al., 2002). When this happens in the absence of a concomitant inflammatory stimulus, the result is the induction of immune tolerance . On the other hand, when the antigen is sent to these same cells in the presence of an inflammatory stimulus, the result is the induction of a strong immune response. The targeting of antigen to DCs in vivo is accomplished by administering low doses of a recombinant chimeric protein consisting of a monoclonal antibody specific for receptors on the surface of DCs fused with the antigen of interest. Currently we are using monoclonal antibodies that have the ability to bind to the receptor DEC 205 ...
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.. ...
Fooling the Virus: The Fusion protein as Virus-Specific Therapeutic An ACE2 A fusion protein of ACE2 with an Immunogenic Component Project ID : 47-2020-10877
USP39 Polyclonal Antibody (CAB9582)OverviewTitle:USP39 Polyclonal Antibody (CAB9582)Size:100µLCode:CAB9582Host Species:RabbitPurification:Affinity purificationIsotype:IgGBackgroundN/AImmunogen InformationImmunogen:Recombinant fusion protein containing a ...
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
The study is a Phase 1b open label, non-randomized, single institution clinical trial that is designed to evaluate the safety and tolerability of three repeat
RBB 001, a recombinant fusion protein, is a targeted cytoprotectant in development with Rubicon Biotechnology for the treatment of myocardial or cerebral
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.
C9orf125 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag14695
P27; KIP1 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag2280
CRISPR prime editing uses pegRNA and a reverse transcriptase-Cas9 nickase fusion protein to edit DNA and has low off-target rates
The recombinant Human Osteocrin is produced with N-terminal fusion of His Tag. The Human Osteocrin His-Tagged Fusion Protein is 13.6 kDa.
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
Protocol Add 2 µl of the substrate stock solution to 18 µl of protein sample containing a SNAP-tag fusion protein in an appropriate buffer (see notes)
TY - JOUR. T1 - Chimeric fusion proteins - Diphtheria toxin-based. AU - Frankel, A. E.. AU - Powell, B. L.. AU - Vallera, D. A.. AU - Neville D.M., Jr. PY - 2001. Y1 - 2001. N2 - Most cancer patients receive chemotherapy drugs that target DNA or the cell division apparatus. Many of these patients develop multidrug-resistant tumor cells, thus, novel methods to overcome drug resistance are needed. One approach is to target tumor cell protein synthesis. Peptide toxins, which catalytically inactivate protein synthesis, have been re-engineered to selectively bind and intoxicate tumor cells. Diphtheria toxin (DT), a member of the class of peptide toxins, has been subjected to structural and genetic analysis and protein engineering for several decades. In this review, we will examine the structure, function, synthesis and pharmacology of anticancer DT conjugates.. AB - Most cancer patients receive chemotherapy drugs that target DNA or the cell division apparatus. Many of these patients develop ...
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 ...
TY - JOUR. T1 - Effect of SBDs position in fusion proteins on activity and binding properties. AU - Ji, Q.. AU - Vincken, J.P.. AU - Raemakers, C.J.J.M.. AU - Suurs, L.C.J.M.. AU - Visser, R.G.F.. PY - 2005. Y1 - 2005. M3 - Comment/Letter to the editor. VL - 28. SP - 1. EP - 5. JO - Journal of Nanjing Normal university: Natural Science Edition. JF - Journal of Nanjing Normal university: Natural Science Edition. SN - 1001-4616. IS - 1. ER - ...
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 ...
We have obtained transgenic mice in which an erythropoietin-SV40 virus T antigen fusion gene is homologously recombined into the native Epo locus. This gene is expressed in a tissue-specific manner closely resembling that of the native Epo gene. Immunohistochemical detection of SV40 T antigen has been used to characterize the hepatic cell populations expressing the transgene. In mice stimulated by anaemia or hypobaric hypoxia, SV40 T antigen was demonstrated in two liver cell populations: a subset of hepatocytes and a nonparenchymal cell type. Immunohistochemical and ultrastructural characterization of these cells by light and electron microscopy showed the nonparenchymal cell type to be the Ito cells, which lie in a persinusoidal position within the space of Disse. We therefore conclude that Ito cells are the nonhepatocytic source of liver Epo production. These cells show many similarities to the Epo-producing fibroblastoid interstitial cells of the kidney.
New preclinical research in animal models finds that infusing a specific protein into scar tissue after a heart attack improves and speeds up the recovery of the heart. According to the American Heart Association (AHA), around 605,000 people in the United States have a new heart attack each year, and approximately 200,000 experience a recurrent attack.. Reperfusion, which is a technique that frees up the flow of oxygen to the hearts tissue, is a common form of treatment after a heart attack. However, up to one-quarter of people who undergo reperfusion develop heart failure within a year.. So, researchers led by James Chong - an associate professor at the University of Sydney in Australia - have explored an alternative treatment that targets the scar tissue that forms after a heart attack.. Chong and colleagues evaluated the therapeutic potential of a protein therapy called recombinant human platelet-derived growth factor-AB (rhPDGF-AB).. As its name suggests, rhPDGF-AB is a recombinant growth ...
Expression In Bacteria Of Beta-Galactosidase Fusion Proteins Carrying Antigenic Determinants Of The 2 X-Gene Products Of Bovine Leukemia- ...
The global Spinal Fusion Systems Market report offers precise analytical information about the Spinal Fusion Systems market. The market experts and proficient analysts generate the information based on the past and current situation of Spinal Fusion Systems market, various factors affecting the growth trajectory, global sales, demand, total revenue generated, and capitalization of the market. Moreover, the report delivers a summarized assessment of the impact of federal policies and regulations on market operations. It also comprises detailed information pertaining to the Spinal Fusion Systems markets current dynamics. The global Spinal Fusion Systems market acts as a huge platform that offers several opportunities for many reputed firms, organizations, manufacturers, vendors, and suppliers Medtronic, Johnson & Johnson, Zimmer Biomet, Benvenue Medical, SeaSpine Holdings Corporation, Alphatec, Orthofix, Stryker to compete with each other to become one of the globally and regionally leading ...
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...
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
Title: Selective Chemokine Receptor-Targeted Depletion of Pathological Cells as A Therapeutic Strategy for Inflammatory, Allergic and Autoimmune Diseases. VOLUME: 3 ISSUE: 3. Author(s):John R. McDonald. Affiliation:Osprey Pharmaceuticals Limited, 7150 Frederick, Banting, d, St. Laurent, QC H4S 2A1, Canada.. Keywords:Chemokine, fusion protein, monoclonal antibody, immunotoxin, allergic, autoimmune, inflammation, cancer, bispecific antibodies, ribosome inactivating protein. Abstract: Targeting cell surface antigens or receptors with lytic monoclonal antibodies and specific ligand-directed fusion proteins in order to eliminate cancer cells has been in development for at least forty years. More recently, leukocyte populations known to drive a host of allergic, autoimmune and inflammatory diseases have been targeted. For fusion protein constructs, a number of different classes of cellular toxins have been fused to a variety of ligands such as monoclonal antibodies, growth factors and cytokines. ...
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.
Elimination of regulatory T lymphocytes may provide a way to break self-tolerance and unleash the anti-tumor properties of circulating lymphocytes. The use of fusion proteins, which link cytotoxic molecules to receptor targets, provides one approach to this problem. This study examined the ability o …
Acute myeloid leukemia (AML) is a disease that is characterized by uncontrolled proliferation of clonal neoplastic cells and accumulation in the bone marrow of blasts with an impaired differentiation program. AML accounts for approximately 80% of all adult leukemias and remains the most common cause of leukemia death. Two major types of genetic events have been described that are crucial for leukemic transformation. A proposed necessary first event is disordered cell growth and upregulation of cell survival genes. The most common of these activating events were observed in the RTK Flt3, in N-Ras and K-Ras, in Kit, and sporadically in other RTKs. Alterations in myeloid transcription factors governing hematopoietic differentiation provide second necessary event for leukemogenesis. Transcription factor fusion proteins such as AML-ETO, PML-RARalpha or PLZF-RARalpha block myeloid cell differentiation by repressing target genes. In other cases, the transcription factors themselves are mutated ...
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, ...
A recombinant fusion proteins (BBG2Na) comprising the central conserved website of the respiratory syncytial computer virus subgroup A (RSV-A) (Long) G protein (residues 130 to 230) and an albumin binding website of streptococcal protein G was shown previously to protect mouse top (URT) and lower (LRT) respiratory tracts against intranasal RSV challenge (U. of the implicated epitopes in the context of the whole computer virus. However, Pepscan analyses of RSV-seropositive human being sera revealed that from the murine B-cell defensive epitopes (protectopes) that mapped towards the central conserved domains had been recognized in guy. Should these murine protectopes end up being implicated in individual LRT security also, their clustering throughout the highly conserved cysteine noose region shall possess important implications for the introduction of RSV vaccines. Respiratory syncytial trojan (RSV) is an associate Rabbit polyclonal to PPAN. from the genus as well as the family members had been ...
A recombinant fusion proteins (BBG2Na) comprising the central conserved website of the respiratory syncytial computer virus subgroup A (RSV-A) (Long) G protein (residues 130 to 230) and an albumin binding website of streptococcal protein G was shown previously to protect mouse top (URT) and lower (LRT) respiratory tracts against intranasal RSV challenge (U. of the implicated epitopes in the context of the whole computer virus. However, Pepscan analyses of RSV-seropositive human being sera revealed that from the murine B-cell defensive epitopes (protectopes) that mapped towards the central conserved domains had been recognized in guy. Should these murine protectopes end up being implicated in individual LRT security also, their clustering throughout the highly conserved cysteine noose region shall possess important implications for the introduction of RSV vaccines. Respiratory syncytial trojan (RSV) is an associate Rabbit polyclonal to PPAN. from the genus as well as the family members had been ...
A no-observable-adverse-effect level is established in the Rhesus monkey for the acute administration of the HIRMAb-GDNF fusion protein. The fusion protein targeting the insulin receptor has a PK profile similar to a classical small molecule.
Mouse monoclonal antibody raised against partial synthetic protein of Pick1. Recombinant fusion protein corresponding to amino acids 101-130 of rat Pick1. (MAB11625) - Products - Abnova
Mouse monoclonal antibody raised against recombinant TFAP2C. Recombinant fusion protein corresponding to TFAP2C. (MAB7289) - Products - Abnova
Zenix SEC-300 (3 µm, 300 Å) column delivers baseline separation of Fc fusion protein, its oligomer, and impurity. With the addition of arginine, the hydrophobic interaction between Fc fusion protein and column resin is minimized. ...
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…. ...
In this article we analyze protein:protein interactions and enzyme activity for several fusion proteins, and show that HaloTag fusion proteins bound to HaloLink Resin maintain function.
Studies using PKC regulatory/catalytic domain chimeras have underscored the complexity of PKC functions in relation to its structural domains. In previous reports, we and others showed that certain features of isozyme-specific PKC functions could be attributed to the catalytic domain only. These include the PKC-δ-mediated PMA-induced macrophage differentiation of 32D cells (14), the tumorigenicity of PKC-ε-overexpressing NIH 3T3 cells (15), the PKC-βII-mediated growth promotion in K-562 cells (26), and the protection of PKC-δ from down-regulation induced by bryostatin 1 in NIH 3T3 cells (17). However, in some cases, both the regulatory and the catalytic domains contribute to the isoform-specific effects (15, 18, 27). Further mapping of the structural domains beyond the catalytic and regulatory regions is essential to clearly determine the function of each structural domain and to understand how individual domains interact with each other to regulate PKC function.. Previous studies on the ...
Caltag Medsystems supply a wide range of fusion proteins for cancer research, neurobiology, metabolism, apoptosis, cell biology, immunology, infectious diseases
The recombinant human ACVR1-Fc fusion protein is expressed as a 331amino acid protein consisting of Met21 - Glu123 region of ACVR1 (UniProt accession #Q04771) and a C-terminal Fc fusion from human IgG1, which exists as a dimer under non-reducing condition.
Raw fusion protein powder experience: You have to avoid these #errors, then #successes are already possible after 17 days ✚ the big test here
POMPEIA, C; ORTIS, F; ARMELIN, M C S. Use of pex and pgex bacterial heterologous protein expression systems for recombinant oncoprotein production and antisera generation. Biotechnology and Applied Biochemistry, San Diego, v. 25, p. 207-15, 1997 ...
Get epitope-tagging technology which can provide you a powerful means to functionally analyze your protein of interest without the need for an antibody specific to each new protein under study. pCMV-3Tag vectors have three copies of the epitope tag in a variety of configurations to prove a stronger signal in immmunological assays.
Sigma-Aldrich offers abstracts and full-text articles by [Mingjun Liu, Jinbao Zong, Zimin Liu, Ling Li, Xu Zheng, Bin Wang, Guirong Sun].
This unit includes protocols for the analysis of the targeting properties of Fc chimeric proteins and antibodies in mice in vivo
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
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