38559 Risultati per: "ProSci Inc."

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Programmed cell death protein 1(PDCD1) is a single-pass type I membrane protein and contains 1 Ig-like V-type domain. PD-1 is a member of the extended CD28/CTLA-4 family of T cell regulators. PDCD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN- gamma by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PDCD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PDCD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.

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Interleukin-18-binding protein, also known as Tadekinig-alfa and IL18BP, contains 1 Ig-like C2-type domain. IL18BP is constitutively expressed and secreted in mononuclear cells. IL18BP functions as an IL18 inhibitor. IL18BP binds to IL18, prevents the binding of IL18 to its receptor, and thus inhibits IL18-induced IFN-gamma production. It has been shown that IL18BP may be a promising molecular approach to inhibit neointimal hyperplasia and arteriosclerosis progression following coronary and peripheral angioplasty.

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Integrin alpha-5 belongs to the Integrin alpha chain family and contains 7 FG-GAP repeats. Integrin alpha-5 joins with Integrin- beta 1 to form a fibronectin and laminin receptor which recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. It is expressed on fibroblasts, endothelial cells, peripheral T cells and platelets. Integrin alpha-5 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains. In addition to adhesion, ITGA5 participates in cell-surface mediated signalling.

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C10orf49 is a secreted protein which encoded by the UCMA gene. It is a member of the UCMA family. C10orf49 is predominantly expressed in resting chondrocytes. It may be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.

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Transthyretin is a secreted and cytoplasm protein which belongs to the Transthyretin family. Transthyretin is detected in serum and cerebrospinal fluid (at protein level). It is highly expressed in choroid plexus epithelial cells. It is also detected in retina pigment epithelium and liver. Each monomer of Transthyretin has two 4-stranded beta sheets and the shape of a prolate ellipsoid. Antiparallel beta-sheet interactions link monomers into dimers. A short loop from each monomer forms the main dimer-dimer interaction. These two pairs of loops separate the opposed, convex beta-sheets of the dimers to form an internal channel. Defects in Transthyretin are the cause of amyloidosis type 1 (AMYL1) which is a hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system.

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Bonzo Antibody: Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, and CCR2b in the chemokine receptor family have been identified as HIV coreceptors. An orphan G protein-coupled receptor was recently cloned and designated Bonzo, STRL33 and TYMSTR, and identified as HIV and SIV coreceptor. Bonzo/STRL33 serves as coreceptor for SIV, HIV-2 and HIV-1. The messenger RNA of Bonzo/STRL33 is expressed in lymphoid tissues and activated peripheral blood lymphocytes.

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Anti-Enterococcus sp Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

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Anti-Neisseria meningitidis Rabbit Polyclonal Antibody (Biotin)

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Anti-Enterococcus sp Rabbit Polyclonal Antibody

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IRF6 is a member of the interferon regulatory transcription factor (IRF) family. Family members share a highly-conserved N-terminal helix-turn-helix DNA-binding domain and a less conserved C-terminal protein-binding domain. Mutations in its gene can cause van der Woude syndrome and popliteal pterygium syndrome. This protein is involved in palate formation.The protein encoded by this gene shares strong similarity with Saccharomyces cerevisiae Cdc23, a protein essential for cell cycle progression through the G2/M transition. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eucaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction.

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IRF7 Antibody: Interferons (IFNs) are involved in a multitude of immune interactions during viral infections and play a major role in both the induction and regulation of innate and adaptive antiviral mechanisms. During infection, host-virus interactions signal downstream molecules such as transcription factors such as IFN regulatory factor-3 (IRF3) which can act to stimulate transcription of IFN-a/b genes. IRF7 has been shown to play a role in the transcriptional activation of virus-inducible cellular genes, including interferon beta chain genes. IRF7 play a major role in the innate immune pathway, interacting with the Toll-like receptor (TLR) adaptor proteins MyD88 and Tirp/TRAM and functioning as an intermediate TLR4 and TLR9 signaling. There are at least four differentially spliced isoforms of IRF7, although their function has not been clearly established.

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Anti-Epstein-Barr Virus Mouse Monoclonal Antibody

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NEUCRIN Antibody: Neucrin, also known as Draxin, is a repulsive guidance protein for the spinal cord and forebrain commissures. It is thought to act as an antagonist of canonical Wnt signaling by inhibiting the stabilization of cytosolic beta-catenin. Ectopically expressed neucrin inhibited growth or caused misrouting of chick spinal cord commissural axons in vivo while Neucrin-null mice showed defasciculation of spinal cord commissural axons and an absence of all forebrain commisures. Other experiments in mice have shown that olfactory bulb axonal outgrowth is inhibited by Neucrin, suggesting that Neucrin functions as an inhibitory guidance cue for olfactory bulb axons.

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Anti-Influenza Goat Polyclonal Antibody (Biotin)

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ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

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Human recombinant Bace12 (from HEK293 cells)

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Nicotinamide phosphoribosyltransferase (Nampt; pre-B cell colony-enhancing factor; PBEF; Visfatin) is an 52kDa adipokine secreted by adipose tissue and involved in the biosynthesis of nicotinamide adenine dinucleotide (NAD+). Two forms of Nampt exist, an intracellular form (iNampt) and an extracellular form (eNampt). While the function of iNampt as an essential and rate-limiting NAD+ biosynthetic enzyme is well established, the physiological role of eNampt is still a matter of debate. Nampt has various functions, including the promotion of vascular smooth muscle cell maturation and inhibition of neutrophil apoptosis. It activates insulin receptor and has insulin-mimetic effects, lowering blood glucose and improving insulin sensitivity. The protein is highly expressed in visceral fat and serum levels of the protein correlate with obesity.

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Bactericidal permeability-increasing protein(BPI for short), is a secreted protein which belongs to the BPI/LBP/Plunc superfamily, BPI/LBP family. It exists as a monomer or a disulfide-linked homodimer. The cytotoxic action of BPI is limited to many species of Gram-negative bacteria. This specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. BPI has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, and this activity is inhibited by LPS from P.aeruginosa.

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Protein Kinase C and Casein Kinase Substrate in Neurons Protein 2 (PACSIN2) is a member of the PACSIN family. PACSIN2 is localized to the plasma membrane via its coiled-coil domain. PACSIN2 is widely expressed and contains one FCH domain and one SH3 domain. PACSIN2 forms homo- and hetero-aggregates with other PACSINs. PACSIN2 may play a role in vesicle formation and transport. In addition, PACSIN2 is involved in linking the actin cytoskeleton with vesicle formation by regulating tubulin polymerization.

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Strongly similar to rat latexin (TCI, Rn.11404); may be a tissue carboxypeptidase inhibitor.

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At least 23 different variants of IFN- alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN- alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN- alpha subtypes only differ in their sequences by one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

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G-CSF is a hematopoietic growth factor that stimulates the development of committed progenitor cells to neutrophils and enhances the functional activities of the mature end-cell. It is produced in response to specific stimulation by a variety of cells including macrophages, fibroblasts, endothelial cells and bone marrow stroma. G-CSF is being used clinically to facilitate hematopoietic recovery after bone marrow transplantation. Human and murine G-CSF are cross-species reactive. Recombinant human G-CSF is an 18.7 kDa protein consisting of 174 amino acid residues.

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ANGPTL7 (Angiopoietin-like protein 7) is expressed in various tissues and regulates angiogenesis. Human ANGPTL7 was characterised as a potent target gene of the WNT/beta-catenin signalling pathway, and is a pharmacogenomics target in the fields of oncology and regenerative medicine. Overexpression of ANGPTL7 increases collagen expression and might exert a pathogenic role in glaucoma.

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Syntenin-1 is a molecule linking syndecan-mediated signalling to the cytoskeleton. Syntenin-1 is primarily localised to membrane-associated adherens junctions and focal adhesions but also found at the endoplasmic reticulum and nucleus. The syntenin protein contains tandemly repeated PDZ domains that bind the cytoplasmic, C-terminal domains of a variety of transmembrane proteins. Syntenin-1 may affect cytoskeletal-membrane organisation, cell adhesion, protein trafficking, and the activation of transcription factors. It seems to function as an adapter protein, in adherens junctions may function to couple syndecans to cytoskeletal proteins or signalling components. Syntenin-1 seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA) and play a role in vesicular trafficking.

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Human recombinant Car (from HEK293 cells)

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Microtubule-Associated Proteins 1A/1B Light Chain 3A (MAP1LC3A) belongs to the MAP1 LC3 family. MAP1LC3A is found most abundantly in the heart, brain, liver, skeletal muscle, and testis. But it is absent in the thymus and peripheral blood leukocytes. MAP1LC3A is thought to take part in the formation of autophagosomal vacuoles and is one of the light chain subunits that functions together with both MAP1A and/or MAP1B. In addition, MAP1A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity.

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TMIGD2 is a single-pass type I membrane protein, which contains one Ig-like (immunoglobulin-like) domain. It is widely expressed in many tissues, such as epithelial, endothelial cells and lung. However, it isn’t detected in thyroid, cerebellum, thymus and cerebral cortex. TMIGD2 can form homophilic interactions that could regulate cell-cell interaction. It Interacts with CACNB2, DST, MIA and NCKIPSD. It is shown that TMIGD2 plays a role in cell-cell interaction, cell migration, and angiogenesis.

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Cathepsin E is encoded by the ctse gene, exists in the homodimer forms, belongs to the peptidase A1 family. Cathepsin E high expressed in the stomach, clara cells and alveolar macrophages of lung, brain microglia, spleen and activated B-lymphocytes. Cathepsin E may involve in the processing of antigenic peptides during MHC class II-mediated antigen presentation, play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain.

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Retinol Binding Protein 4 (RBP4) is a member of the Lipocalin family and in the blood. RBP4 is the specific vector for retinol. RBP4 is expressed and secreted by adipose tissue, and is associated with insulin resistance. RBP4 delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin to prevents its loss by filtration through the kidney glomeruli. Defects in RBP4 cause retinol-binding protein deficiency and can cause night vision problems.

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Melanoma Inhibitory Activity Protein (MIA) is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells, which was the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family: MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion and promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. The protein MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis.