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Proteins are used in routine laboratory procedures such as binding enzymes or coupling peptides to carrier proteins. These kits, mixture solutions, and collagen matrices fulfill a myriad of essential laboratory functions for developing relationships between proteins and other cellular components. The stimulating proteins offered have various amino acid arrangements and functions to fulfill any sample manipulation for testing purposes in any field.
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Description:
Serum Amyoid P Component (SAP) is a monomeric 25 kDa secreted serum glycoprotein that belongs to the pentraxins family. The members of pentaxin superfamily be characterised by calcium dependent ligand binding and distinctive flattened beta -jellyroll structure similar to that of the legume lectins. SAP is a non-fibrillar component, it can interact with DNA and histones. It regulates the solubility of amyloid fibrils and protects them from degradation by proteolytic enzymes and phagocytic cells. SAP scavenge nuclear material released from damaged circulating cells. It has been proposed that SAP may function as an opsonin for a variety of ligands including autoantigens, apoptotic cells, chromatin and micro-organisms.
Description:
Multiple Inositol Polyphosphate Phosphatase 1/MINPP1 is an enzyme that removes 3-phosphate from inositol phosphate substrates. MINPP1 also converts 2,3 bisphosphoglycerate (2,3-BPG) to 2-phosphoglycerate. MINPP1 is synthesized as a 487 amino acid precursor that contains an 30 amino acid signal peptide and a 457 amino aicd mature chain. MINPP1 is widely expressed with the highest levels found in kidney, liver and placenta. It acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). MINPP1 may play a role in bone development (endochondral ossification).
Description:
Protein Disulfide-Isomerase-Like Protein of the Testis (PDILT) is a protein that belongs to the protein disulfide isomerase family. Human PDILT is synthesized as a 584 amino acid precursor that contains an 20 amino acid signal sequence and a 564 amino acid mature chain. PDILT contains 1 thioredoxin domain lacks the conserved redox-active Cys at position 417 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity. PDILT is an enzyme in the endoplasmic reticulum in eukaryotes. It is not a disulfide-linked homodimer. The PDILT protein can interacts with ERO1L and CLGN. PDILT probable redox-inactive chaperone involved in spermatogenesis.
Description:
beta -2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules, involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases, various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.
Description:
CD279 (Programmed Cell Death Protein 1; PD-1) is a type I transmembrane protein belonging to the CD28/CTLA-4 family of immunoreceptors that mediate signals for regulating immune responses. Members of the CD28/CTLA-4 family have been shown to either promote T cell activation (CD28 and ICOS) or downregulate T cell activation (CTLA-4 and PD-1). CD279 is expressed on activated T cells, B cells, myeloid cells and on a subset of thymocytes. In vitro, ligation of CD279 inhibits TCR-mediated T cell proliferation and production of IL-1, IL-4, IL-10 and IFN-gamma. In addition, CD279 ligation also inhibits BCR mediated signallling. CD279 deficient mice have a defect in peripheral tolerance and spontaneously develop autoimmune diseases.
Description:
Apolipoprotein A1 (APOA1) is a secreted protein which belongs to the Apolipoprotein A1/A4/E family. APOA1 is the major protein component of high density lipoprotein (HDL) in plasma. APOA1 plays a critical role in various biological processes, such as Cholesterol metabolism, Lipid metabolism and transport, Steroid metabolism. APOA1 promotes cholesterol efflux from tissues to the liver and thus helps to clear cholesterol from arteries. Defects in this gene resulted in HDL deficiencies, including Tangier disease (TGD), systemic non-neuropathic amyloidosis, premature coronary artery disease, hepatosplenomegaly and progressive muscle wasting and weakness. In addition, ApoA-I is implicated in the anti-endotoxin function of HDL via interaction with lipopolysaccharide or endotoxin.
Description:
Oxidized Low-Density Lipoprotein Receptor 1 (Ox-LDL Receptor 1) is a secreted, single-pass type II membrane protein which belongs to the C-type lectin superfamily. Ox-LDL Receptor 1 is expressed at high levels in endothelial cells and vascular-rich organs such as placenta, lung, liver, brain, aortic intima, bone marrow, spinal cord and substantia nigra. The expression of Ox-LDL Receptor 1 is induced by inflammatory cytokines such as TNF, IFNG and IL6 by pathological conditions, such as hyperlipidemia, hypertension and diabetes mellitus. Ox-LDL Receptor 1 mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (OxLDL) by vascular endothelial cells. Ox-LDL Receptor 1 association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. Ox-LDL Receptor 1 also binds to oxLDL, which acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. It also participates in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation.
Description:
CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.
Description:
Allograft Inflammatory Factor 1 (AIF1) contains two EF-hand domains and exists as a homodimer. AIF1 can be detected in T-lymphocytes and peripheral blood mononuclear cells. AIF1 functions as actin-binding protein that enhances membrane ruffling and RAC activation and can enhance the actin-bundling activity of LCP1. In addition, AIF1 plays a role in RAC signaling and in phagocytosis and may also in macrophage activation and function. AIF1 promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes and plays a role in vascular inflammation.
Description:
Mitochondrial Fission 1 Protein (FIS1) is a member of the FIS1 family. FIS1 is a single-pass membrane protein and contains one TPR repeat. FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 can induce cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. In addition, FIS1 participates in peroxisomal growth and division. The C-terminus of FIS1 is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.
Description:
Mesothelin is a cell surface glycoprotein whose expression is limited to mesothelial cells of the serosa (pleura, pericardium, and peritoneum) and epithelial cells of the trachea, tonsils, fallopian tube, and kidneys. Mesothelin plays an important role in cell survival, proliferation, migration, invasion, tumour progression, and resistance to chemotherapy. The overexpression of mesothelin can activate NF-κB and signal transducer and activator of transcription 3 (Stat3), inhibit apoptotic signalling and TNF- alpha-induced apoptosis, and accelerate the G1–S transition. Mesothelin is also found overexpressed in various cancers, including malignant mesothelioma, pancreatic or ovarian carcinoma, sarcomas and in some gastrointestinal or pulmonary carcinomas. As a result of its limited expression in normal tissues, mesothelin has been reported as an ideal tumour-associated marker for the development of targeted therapy.
Description:
Tumour necrosis factor receptor superfamily member 27, also known as XEDAR and EDA2R, is a type III transmembrane protein of the TNFR (tumour necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain but lacks an N-terminal signal peptide. EDA2R, as well as its paralog, EDAR, binds the ectodysplasin ligands EDA-A2 and EDA-A1, which are two alternatively spliced forms of the EDA gene. Mutations in the EDA gene are associated with the X-linked form of Hypo hidrotic Ectodermal Dysplasia (HED), a disease typically characterized by abnormal hair, teeth and sweat glands.
Description:
IL-1beta is produced by activated macrophages. IL-1beta stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1beta belongs to the IL-1 family of proteins that are involved in the inflammatory response. IL-1beta in most situations requires the inflammasome complex to be cleaved and secreted.
Description:
Interleukin 18 binding protein (IL-18BP) is a physiological inhibitor that acts through binding to the receptor-binding site of IL-18. IL-18 stimulates INF- gamma , which then stimulates 18BP production via NF-κB. The interaction between IL-18 and IL-18BP has a significant role in the inflammation process. IL-18 BPs have four isoforms, a, b, c and d, which are spliced by different ways. The IL-18 BP isoforms a and c each contain one immunoglobulin (Ig)-like C2-type domain which is essential to the binding and neutralizing properties of the binding proteins. The IL-18 BP isoforms b and d lack a complete Ig domain. The expression of IL-18 and the IL-18BP are unidentified in immune tissues such as the spleen, but also in nonimmune cells including keratinocytes.
Description:
Interleukin-22(IL-22) is a member of a group of the IL-10 family, a class of potent mediators of cellular inflammatory responses. IL-22 is produced by activated DC and T cells. IL-22 and IL-10 receptor chains play a role in cellular targeting and signal transduction. It can initiate and regulate innate immune responses against bacterial pathogens especially in epithelial cells such as respiratory and gut epithelial cells. IL-22 along with IL-17 likely plays a role in the coordinated response of both adaptive and innate immune systems. IL-22 also promotes hepatocyte survival in the liver and epithelial cells in the lung and gut similar to IL-10. Biological activity of IL-22 is initiated by binding to a cell-surface complex consisting of IL-22R1 and IL-10R2 receptor chains. IL-22 biological activity is further regulated by interactions with a soluble binding protein, IL-22BP. IL-22BP and an extracellular region of IL-22R1 share sequence similarity. In some cases, the pro-inflammatory versus tissue-protective functions of IL-22 are regulated by cytokine IL-17A.
Description:
Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells, and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils, and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens.
UOM:
1 * 50 µG
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