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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:
Elafin is a secreted protein. Elafin consists of two domains: the transglutaminase substrate domain (cementoin moiety) and the elastase inhibitor domain. The transglutaminase substrate domain serves as an anchor to localize Elafin covalently to specific sites on extracellular matrix proteins. It is shown that Elafin can be used as a biomarker for graft versus host disease of the skin. Elafin is expressed in the skin during wound healing through activation of the epidermal growth factor receptor. Elafin may prevent elastase-mediated tissue proteolysis.
Description:
Cadherin-11 is a type II classical cadherin member of the cadherin superfamily of integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherins interact with themselves in a homophilic manner in connecting cells, and thus contribute to the sorting of heterogeneous cell types. Cadherin-11 contains five cadherin domains and is mainly expressed in the brain. Mature cadherin proteins consists of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. It is shown that Cadherin-11 is a viable molecular target for therapeutic intervention in Glioblastoma multiforme.
Description:
Mouse Cytotoxic Tlymphocyte 4(CTLA-4,CD152), is a type I transmembrane T cell inhibitory molecule. Within the ECD, Mouse CTLA-4 shares 68% aa sequence identity with human. CTLA4 is similar to the T cell costimulatory protein CD28 since both of the molecules bind to CD80 and CD86 on antigen-presenting cells. CTLA4 transmits an inhibitory signal to T cells, whereas CD28 transmits a stimulatory signal. Intracellular CTLA4 is also found in regulatory T cells and may play an important role in their functions. T cell activation through the T cell receptor and CD28 leads to increased expression of CTLA4. Genetic variations of CTLA4 have been associated with susceptibility to systemic lupus erythematosus(SLE), Gravesdisease(GRD), Celiac disease type3(CELIAC3) and Hepatitis B virus infection(HBVinfection).
Description:
Mouse Interleukin 1 receptor, type II (IL1R2) is a cytokine receptor that belongs to the interleukin-1 receptor family. This protein binds interleukin alpha (IL1A), interleukin beta (IL1B), and interleukin 1 receptor, type I (IL1R1/IL1RA), and acts as a decoy receptor that inhibits the activity of its ligands. IL-1R2 structurally consisting of a ligand binding portion comprised of three Ig-like domains, a single transmembrane region, and a short cytoplasmic domain. It is expressed in a variety of cell types including B lymphocytes, neutrophils, monocytes, large granular leukocytes and endothelial cells. Mouse IL1RII shares 59% amino acid sequence homology with human IL1 RII in their extracellular domains. The pleiotropic cytokine IL1 is produced to regulate development and maintenance of the inflammatory responses, and binds to specific plasma membrane receptors on cells. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified, designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1R1 contributes to IL-1 signalling, whereas the IL-1R2 has no signalling property and acts as a decoy for IL-1.
Description:
Natural killer cell receptor 2B4 is also known as NK cell type I receptor protein 2B4 (NKR2B4 or h2B4), SLAM family member 4 (SLAMF4), Signaling lymphocytic activation molecule 4, CD antigen CD244. NKR2B4 / CD244 contains two Ig-like (immunoglobulin-like) domains. CD244 is expressed in spleen, PBL, followed by lung, liver, testis and small intestine. CD244 interacts with CD48. Following phosphorylation, CD244 is able to recruit PTPN11/SHP-2 and SH2D1A/SAP. SLAMF4 modulate other receptor-ligand interactions to enhance leukocyte activation. CD244/2B4 is the only heterophilic receptor of SLAM family.
Description:
Interleukin-1 receptor type 2 (IL1R2) belongs to the interleukin-1 receptor family. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified, designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1 receptor type II is a 68 kDa transmembrane protein found on B lymphocytes, neutrophils, monocytes, large granular leukocytes and endothelial cells. IL1R2 is non-signalling receptor forIL1A, IL1B and IL1RN, reduces IL1B activities. IL1R2 serves as a decoy receptor by competitive binding to IL1B and preventing its binding to IL1R1. IL1R2 modulates cellular response through non-signalling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralisation of IL1B by secreted/soluble receptors.
Description:
Interleukin 6 receptor (IL6R) is also known as CD126 (Cluster of Differentiation 126) , is a potent pleiotropic cytokine that regulates cell growth and differentiation of various tissues, and is known particularly for its role in the immune response and acute phase reactions. IL6R is a protein complex consisting of a IL-6 receptor subunit (IL6R) and interleukin 6 signal transducer Glycoprotein 130. IL6R also denotes the human gene encoding this subunit. Alternatively spliced transcript variants encoding distinct isoforms have been reported. IL6R subunit also shared by many other cytokines. The soluble form of IL6R arises from proteolytic cleavage of membrane-bound IL6Rα, and acts agonistically by making the IL6 ligand accessible to the signal transducer gp130. Dysregulated production of IL6 and IL6R are implicated in the pathogenesis of several inflammatory diseases and malignancies such as multiple myeloma, rheumatoid arthritis, or osteoporosis, and it has been reported that a humanised anti-IL6R monoclonal antibody is a promising agent applicable to the therapeutic approach for IL6 driven diseases. Interleukin-6 receptor has been shown to interact with Interleukin 6 and Ciliary neurotrophic factor.
Description:
Interleukin-2 receptor subunit alpha (IL2RA) is also known as IL-2R subunit alpha, IL-2-RA, IL2-RA, TAC antigen, p55, CD antigen CD25, is a type I transmembrane glycoprotein. IL2RA is expressed on activated T cells and regulatory T cells, and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covelently with the IL2 receptor beta and gamma chain, and subsequently initiates the intacellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling.
Description:
Interleukin-1 beta (IL-1β) is also known as catabolin, is a cytokine protein that in humans is encoded by the IL1B gene. IL-1β precursor is cleaved by caspase 1 (interleukin 1 beta convertase). Cytosolic thiol protease cleaves the product to form mature IL-1 beta. IL1β are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL1α and IL1β are regulated independently, they bind to the same receptor and exert identical biological effects. IL-1β is a member of the interleukin 1 cytokine family. This cytokine is produced by activated macrophages as a proprotein, which is proteolytically processed to its active form by caspase 1 (CASP1/ICE). This cytokine is an important mediator of the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. The induction of cyclooxygenase-2 (PTGS2/COX2) by this cytokine in the central nervous system (CNS) is found to contribute to inflammatory pain hypersensitivity. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2.
Description:
tumour necrosis factor receptor superfamily member 13B, also known as TNFRSF13B or more commonly as TACI (transmembrane activator and CAML interactor), is a transmembrane receptor protein found predominantly on the surface of B cells, which are an important part of the immune system.
Description:
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.
Description:
LMIR1, also termed CD300a, is a type I transmembrane glycoprotein with a single IgV-like extracellular domain and an extended membrane proximal region that links the immunoglobulin (Ig) and transmembrane domains and belongs to the immunoglobulin superfamily. The intracellular domain of LMIR1 contains several immunoreceptor tyrosine-based inhibition motifs (ITIMs). When cross-linked, it will be tyrosine phosphorylated and capable of recruiting tyrosine phosphatases (SHP-1, SHP-2) and inositol polyphosphate 5-phosphatase, SHIP. LMIR1 will regulate mast cell-mediated inflammatory responses. LMIR1 is broadly expressed on myeloid and lymphoid cells, and its expression is differentially regulated depending on the cell type.
Description:
Pentraxin 2 (PTX2), also known as Serum amyloid P (SAP), is a highly conserved, naturally circulating plasma protein and a soluble pattern recognition receptor of the innate immune system. The unique binding activities indicated that it may play an important role in the removal of damaged tissue. PTX2 belongs to the pentraxin family, is universally present in amyloid deposits. Mouse with targeted deletion of the PTX2 gene shows retarded and reduced induction of experimental reactive systemic (AA type) amyloidosis confirmed that it does indeed contribute to pathogenesis of amyloidosis and is a valid therapeutic target. In recent discovery, PTX2 can be used as a powerful antifibrotic agent to regulate certain monocyte differentiation states.
Description:
Mesothelin (MSLN) is also known as CAK1 antigen, Pre-pro-megakaryocyte-potentiating factor, which belongs to the mesothelin family. Mesothelin / MSLN can be proteolytically cleaved into the following two chains by a furin-like convertase: Megakaryocyte-potentiating factor (MPF) and the cleaved form of mesothelin. Both MPF and the cleaved form of mesothelin are N-glycosylated. Mesothelin / MSLN can interacts with MUC16. The membrane-anchored forms of MSLN may play a role in cellular adhesion. MPF potentiates megakaryocyte colony formation in vitro.
Description:
Mesothelin (MSLN) is also known as CAK1 antigen, Pre-pro-megakaryocyte-potentiating factor, which belongs to the mesothelin family. Mesothelin / MSLN can be proteolytically cleaved into the following two chains by a furin-like convertase: Megakaryocyte-potentiating factor (MPF) and the cleaved form of mesothelin. Both MPF and the cleaved form of mesothelin are N-glycosylated. Mesothelin / MSLN can interacts with MUC16. The membrane-anchored forms of MSLN may play a role in cellular adhesion. MPF potentiates megakaryocyte colony formation in vitro.
Description:
Syndecan-1 is a single-pass type I membrane protein that belongs to the syndecan proteoglycan family. The syndecans mediate cell binding, cell signaling, and cytoskeletal organization and syndecan receptors are required for internalization of the HIV-1 tat protein. Human SDC1 is synthesized as a 310 amino acid precursor that contains a 22 amino acid signal sequence, and a 288 amino acid mature chain. The Syndecan-1 protein functions as an integral membrane protein and participates in cell proliferation, cell migration and cell-matrix interactions via its receptor for extracellular matrix proteins. Altered Syndecan-1 expression has been detected in several different tumor types.
UOM:
1 * 50 µG
Promotion
,PRSI91-771EA
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