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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:
VEGF165 is the most abundant splice variant of VEGF-A. VEGF165 is produced by a number of cells including endothelial cells, macrophages and T cells. VEGF165 is involved in angiogenesis, vascular endothelial cell survival, growth, migration and vascular permeability. VEGF gene expression is induced by hypoxia, inflammatory cytokines and oncogenes. VEGF165 binds to heparan sulfate and is retained on the cell surface and in the extracellular matrix. VEGF165 binds to the receptor tyrosine kinases, VEGFR1 and VEGFR2. VEGF165 is the only splice variant that binds to co-receptors NRP-1 and NRP-2 that function to enhance VEGFR2 signaling. Binding of VEGF165 to VEGFR1 and VEGFR2 leads to activation of the PI3K/AKT, p38 MAPK, FAK and paxillin. VEGF plays a key role in tumor angiogenesis in many cancers.
Description:
V-set and immunoglobulin domain-containing protein 4 (VSIG4) is also known as Protein Z39Ig, is a type I transmembrane glycoprotein. VSIG4 is a B7 family-related protein and an Ig superfamily member. VSIG4 contains two Ig-like (immunoglobulin-like) domains. VSIG4 is abundantly expressed in several fetal tissues. In adult tissues, the highest expression of VSIG4 is in lung and placenta. VSIG4 functions as a negative regulator of T cell activation, and may be involved in the maintenance of peripheral T cell tolerance, and is also identified as a potent suppressor of established inflammation. VSIG4 is a phagocytic receptor, strong negative regulator of T-cell proliferation and IL2 production.
Description:
Vascular cell adhesion protein 1 (VCAM1) is also known as CD106, INCAM-100 and L1CAM, is a cell surface sialoglycoprotein belonging to the immunoglobulin superfamily. VCAM1 / CD106 contains 7 Ig-like C2-type (immunoglobulin-like) domains. CD106 / VCAM-1 is expressed on inflammed vascular endothelium, as well as on macrophage-like and dendritic cell types in both normal and inflammed tissue. L1CAM / VCAM-1 is Important in cell-cell recognition and appears to function in leukocyte-endothelial cell adhesion. CD106 / VCAM1 interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1 / VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation. INCAM-100 / VCAM1 binds to ECMV-D capsid proteins and acts as a receptor for this virus.
Description:
PARP-3 [ARTD3] is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signalling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.
Description:
CREB-binding protein acetylates histones, giving a specific tag for transcriptional activation. It also acetylates non-histone proteins, like NCOA3 and FOXO1. It binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300.
Description:
NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.
Description:
C-type lectin superfamily 4, member G (CLEC4G) is also known as liver and lymph node sinusoidal endothelial cell C-type lectin (LSECtin), which is a member of subgroup II of the C-type (Ca2+-dependent) lectin superfamily. CLEC4G / LSECtin binds to mannose, GlcNAc, and fucose in a Ca2+-dependent manner. In addition, CLEC4G / LSECtin has the ability to bind to surface glycoproteins of enveloped viruses. In particular, interaction of LSECtin with the surface glycoproteins of severe acute respiratory syndrome (SARS) coronavirus and Ebola virus has been described, and LSECtin-mediated infection of cells by Ebola virus has been demonstrated.
Description:
Cartilage oligomeric matrix protein (COMP) is also known as Thrombospondin-5 (TSP5), EDM1, EPD1, MED, PSACH, THBS5, which belongs to the thrombospondin family. COMP / TSP5 contains 4 EGF-like domains, 1 TSP C-terminal (TSPC) domain, 8 TSP type-3 repeats. Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. COMP may play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. COMP can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Thrombospondin-5 could play a role in the pathogenesis of osteoarthritis. COMP is a marker of cartilage turnover.
Description:
KLK3, also known as APS, is short for Prostate-specific antigen. It is a 261 aa. protein which belongs to the peptidase S1 family and Kallikrein subfamily. This protein has 5 isforms produced by alternative splicing. It is a secreted protein and can forms a heterodimer with SERPINA5 which can inhibit its activity. KLK3 is also strongly inhibited by Zn²⁺, 100 times more abundant in semen than in serum. This inhibition is relieved by exposure to semenogelins, which are avid zinc binders. KLK3 can hydrolyses semenogelin-1 thus leading to the liquefaction of the seminal coagulum.
Description:
Cell surface glycoprotein CD200 Receptor 1 (CD200R1) is the receptor for the CD200 (OX-2) membrane glycoprotein. CD200R1 contains one C2- type Ig-like domain and one V-type Ig-like domain within its extracellular domain and a PTB-signaling motif in cytoplasmic domain. CD200R1 and CD200 associate via their respective N-terminal Ig-like domains. CD200R1 is restricted primarily to mast cells, basophils, macrophages, and dendritic cells. It propagates inhibitory signals despite its lacking a cytoplasmic ITIM (immunoreceptor tyrosinebased inhibitory motif). The receptor-substrate interaction may function as a myeloid downregulatory signal.
Description:
Tumor necrosis factor receptor superfamily member 12A(TNFRSF12A) is also known as Fibroblast growth factor-inducible immediate-early response protein 14, FN14, CD266 antigen and tweak-receptor. TNFRSF12A is a single-pass type I membrane protein, including a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. TNFRSF12A is highly expressed in heart, placenta and kidney. TNFRSF12A can be induced by FGF1 and phorbol ester. TNFRSF12A binds to TWEAK/TNFSF12A to initiate a signal transduction cascade, causing different cellular responses such as cell death, cell proliferation, and angiogenesis.
UOM:
1 * 50 µG
Promotion
,PRSI91-900EA
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