42864 Results for: "ProSci Inc."

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Interleukin 6 (IL-6) is a pleiotropic alpha-helical cytokine that plays important roles in acute phase reactions, inflammation, hematopoiesis, bone metabolism and cancer progression. IL-6 activity is essential for the transition from acute inflammation to either acquired immunity or chronic inflammatory disease. It is secreted by multiple cell types as a 22kDa-28kDa phosphorylated and variably glycosylated molecule. IL-6 induces signallling through a cell surface heterodimeric receptor complex composed of a ligand binding subunit (IL-6R) and a signal transducing subunit (gp130). IL-6 is a key factor for the growth of plasma cells.

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Anti-EPB41L5 Goat Polyclonal Antibody

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IL-6 is reported to be produced by fibroblasts, activated T cells, activated monocytes or macrophages and endothelial cells. It acts upon a variety of cells including fibroblasts, myeloid progenitor cells, T cells, B cells and hepatocytes. In addition, IL-6 appears to interact with IL2 in the proliferation of T lymphocytes. IL-6 potentiates the proliferative effect of IL-3 on multipotential hematopoietic progenitors. IL-6 is a multifunctional 24 kDa protein originally discovered in the medium of RNA stimulated fibroblastoid cells. It is upregulated by IL1, TNF, PDGF, IFN beta, TNF alpha, NGF, IL17 and downregulated by glucocorticoids IL4, TGF beta. IL-6 appears to be directly involved in the responses that occur after infection and cellular injury, and it may prove to be as important as IL1 and TNF alpha in regulating the acute phase response. IL6 has also been implicated in regulating adipose mass.

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Interleukin 5 (IL-5) is a cytokine produced primarily by activated T lymphocytes. It exists as an antiparallel disulfide linked homodimeric glycoprotein with 115 amino acid residues in each chain. Known also as EDF (eosinophil differentiating factor), functions predominantly as an eosinophilopoietic factor. Analysis of its crystal structure reveals a novel two domain structure, with each domain showing significant homology to the cytokine fold in GMCSF, MCSF, IL-2, IL-4 and growth hormone. Human and mouse IL-5 have 70% amino acid sequence homology.

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GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the gaba/benzodiazepine receptor and opening an integral chloride channel.

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GLI1 is a protein which is a member of the Kruppel family of zinc finger proteins. The function of this gene has not been determined; however, it may play a role in normal development gene transcription. Mouse mutation studies indicate possible involvement in human foregut malformation.

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The function remains unknown.

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FUT6 is a Golgi stack membrane protein that is involved in the creation of sialyl-Lewis X, an E-selectin ligand. Mutations in this gene are a cause of fucosyltransferase-6 deficiency. The protein encoded by this gene is a Golgi stack membrane protein that is involved in the creation of sialyl-Lewis X, an E-selectin ligand. Mutations in this gene are a cause of fucosyltransferase-6 deficiency. Two transcript variants encoding the same protein have been found for this gene.

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ACRP30 was identified as a novel adipocyte-specific synthesized and secreted protein with structural resemblance to complement factor C1q. Like adipsin, ACRP30 secretion is induced ~10-fold during adipocyte differentiation. Plasma levels are reduced in obese humans, and low levels are associated with insulin-resistance. Treatment of db/db mice with TZD increased ACRP30 levels.

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Acyl-Protein Thioesterase 2 is a cytoplasmic protein that belongs to the AB Hydrolase 2 family. LYPLA2 is a lysophospholipase and hydrolyses fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. LYPLA2 has hydrolase activity that converts Palmitoyl-protein to palmitate and protein. LYPLA2 regulates the multifunctional lysophospholipids by acting on biological membranes. LYPLA2 participates in Glycerophospholipid metabolism pathway, fatty acid metabolic process and lipid metabolic process.

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Valosin-Containing Protein (VCP) is a nuclear protein that belongs to the AAA ATPase family. VCP is a putative ATP-binding protein involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. It is necessary for the fragmentation of Golgi stacks during mitosis and their reassembly after mitosis. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. VCP participates in the formation of the transitional endoplasmic reticulum (tER) and regulates E3 ubiquitin-protein ligase activity of RNF19A.

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IRF2 encodes interferon regulatory factor 2, a member of the interferon regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of interferons alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4.

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DEK was first identified in a fusion with the CAN nucleoporin protein in a specific subtype of acute myelogenous leukemia. DEK has also been shown to be an autoantigen in patients with pauciarticular onset juvenile rheumatoid arthritis. Further, the last 65 amino acids of DEK can partially reverse the mutation-prone phenotype of cells from patients with ataxia-telangiectasia

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Anti-PKP2 Goat Polyclonal Antibody

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Anti-LAMA5 Goat Polyclonal Antibody

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Anti-PRDM14 Goat Polyclonal Antibody

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ETS1 Protein (ETS1) is a nuclear protein that belongs to the ETS family. Members of this family recognize the core consensus DNA sequence GGAA/T in target genes. Proteins function either as transcriptional activators or repressors of numerous genes. They are involved in stem cell development, cell senescence and death, and tumorigenesis. ETS1 is a transcription factor, containing one ETS DNA-binding domain and one PNT (pointed) domain. it has been shown to interact with TTRAP, UBE2I and Death Associated Protein 6.

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Interleukin-35 is a newest and potent suppressive cytokine of the IL-12 family. Unlike other members of the IL-12 family which are produced mainly by antigen-presenting cells (APCs), IL-35 has been identified as a potentially immunosuppressive cytokine primarily produced by regulatory T (Treg) cells, and to a lesser extent by activated dendritic cells and macrophages. IL-35 is composed of the IL-12 p35 subunit and the IL-27 Epstein–Barr virus-induced protein 3 (EBI3) subunit. IL-35 plays an important role in many disease models and has been recently shown to have additional functions aside from inhibition of proliferation, including inducing its own expression in non-Treg cells.

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CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumour growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.

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SOX9 recognizes the sequence CCTTGAG along with other members of the HMG-box class DNA-binding proteins. It acts during chondrocyte differentiation and, with steroidogenic factor 1, regulates transcription of the anti-Muellerian hormone (AMH) gene. Deficiencies lead to the skeletal malformation syndrome campomelic dysplasia, frequently with sex reversal.

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FOXK2 contains a fork head DNA binding domain. This protein can bind to the purine-rich motifs of the HIV long terminal repeat (LTR), and to the similar purine-rich motif in the interleukin 2 (IL2) promoter. It may be involved in the regulation of viral and cellular promoter elements. Three alternatively spliced transcript variants encoding distinct isoforms have been described.

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Myb-Related Protein B (MYBL2), a member of the MYB family of transcription factor genes, is a nuclear protein involved in cell cycle progression. The encoded protein is phosphorylated by cyclin A/cyclin-dependent kinase 2 during the S-phase of the cell cycle and possesses both activator and repressor activities. It has been shown to activate the cell division cycle 2, cyclin D1, and insulin-like growth factor-binding protein 5 genes. Transcript variants may exist for this gene, but their full-length natures have not been determined.

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Anti-TXNDC5 Goat Polyclonal Antibody

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Anti-RORC Goat Polyclonal Antibody

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Anti-SCOC Goat Polyclonal Antibody

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Anti-ZEB2 Goat Polyclonal Antibody

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The chemokine (C-C motif) ligand 2 (CCL2), also known as monocyte chemoattractant protein (MCP)-1 and small inducible cytokine A2 (SCYA2)), is a small cytokine that belongs to the CC chemokine family responsible for monocyte attraction. Its cognate receptor, CCR2, play a critical role in regulating nociceptive processes during neuropathic pain. Both CCL2 and CCR2 are implicated in induction of autoimmunity. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection. Recently research also showed that CCL2 might be useful as a biomarker of fibrosis as well as a target for therapeutic intervention.

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Fibroblast growth factor 7 (FGF7) is a secreted protein which is mainly located in epithelial cells and belongs to the heparin-binding growth factors family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumour growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. It is possible major paracrine effector of normal epithelial cell proliferation.

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Tumour Necrosis Factor Ligand Superfamily Member 15 (TNFSF15) is a new member of the tumour necrosis factor family. TNFSF15 is predominantly an endothelial cell-specific gene, and recombinant TNFSF15 is a potent inhibitor of endothelial cell proliferation, angiogenesis and tumour growth. TNFSF15 exerts two activities on endothelial cells: early G1 arrest of G0/G1-cells responding to growth stimuli and programmed cell death of proliferating cells. These activities are highly specific to endothelial cells. TNFSF15 is also able to regulate the expression of several important genes involved in angiogenesis. These findings are consistent with the view that TNFSF15 functions as an autocrine cytokine to inhibit angiogenesis and stabilise the vasculature.

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Three receptors for BAFF were recently identified and designated TACI, BCMA and BAFF-R. BAFF-R signaling is essential for B cell development, survival and humoral immune responses.