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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:
Platelet-derived growth factor subunit A (PDGFA), belongs to the PDGF/VEGF growth factor family. PDGFA is a secreted protein, stored in platelet alpha-granules and released by platelets upon wounding. PDGFA is potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. It plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. PDGFA is required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis, normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. It plays an important role in wound healing; Signaling is modulated by the formation of heterodimers with PDGFB.
Description:
Protein S100-A8(Mrp8) contains 2 EF-hand domains and belongs to the S-100 family. Mrp8 binds two calcium ions per molecule with an affinity similar to that of the S-100 proteins. S100 proteins are localised in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. It may function in the inhibition of casein kinase and as a cytokine. Altered expression of this protein is associated with the disease cystic fibrosis.
Description:
neuregulin-1 (heregulin-1，NRG1) is a member of neuregulin family, which is comprised of four genes that encode a large number of secreted or membrane-bound isoforms. All family members share an EGF-like domain that interacts with the ErbB family of tyrosine kinase receptors. NRG1 isoforms can be classified into type I, type II and type III isoforms. NRG1 directs ligand for ERBB3 and ERBB4 tyrosine kinase receptors, concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. NRG proteins show distinct spatial and temporal expression patterns and play important roles during development of both the nervous system and the heart.
Description:
IL2RG contains one fibronectin type-III domain. IL2RG is an important signaling component of many interleukin receptors, including those of interleukin -2, -4, -7 and -21, and is thus referred to as the common gamma chain. IL2RG interacts with SHB upon interleukin stimulation and HTLV-1 accessory protein p12I. Defects in IL2RG are the cause of X-linked combined immunodeficiency (XCID) and severe combined immunodeficiency X-linked T-cell-negative /B-cell-positive / NK-cell-negative (XSCID).
Description:
R-spondin-3 (RSPO3), also known as Protein with TSP type-1 repeat, Roof plate-specific spondin-3, Thrombospondin type-1 domain-containing protein 2, PWTSR, THSD2 and CRISTIN1, is a member of the thrombospondin type 1 repeat supergene family. RSPO3 is a secreted protein and widely expressed in many tissues. RSPO3 contains two Furin-like repeats which have been found in a variety of eukaryotic proteins involved in the mechanism of signal transduction by receptor tyrosine kinases, and one TSP type-1 domain, RSPO3 founctions as a activator of the beta-catenin signaling cascade, leading to TCF-dependent gene activation. Otherwise, RSPO3 may negatively regulate the TGF-beta pathway.
Description:
Ubiquitin-Conjugating Enzyme E2 G2 (UBE2G2) is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation, which belong to the ubiquitin-conjugating enzyme family. It shares 60% and 100% sequence identity with S.cerevisiae Ubc7 and mouse respectively. The UBE2G2 enzyme and the GP78 E3 ligase are active components of endoplasmic reticulum-associated degradation pathway which is essential for the degradation of misfolded ER proteins. The mechanism of K48-linked poly-ubiquitination by UBE2G2/GP78 appears to involve the transfer of preassembled Ub chains from UBE2G2 to lysine residues in a substrate. The E2 and E3 enzymes form a large hetero-oligomer which brings multiple UBE2G2 molecules into close proximity which allows for Ub transfer between neighboring E2s.
Description:
KLKB1 is a 638 amino acids protein that belongs to the peptidase S1 family and plasma kallikrein subfamily. It contains a peptidase S1 domain and four apple domains. The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. It participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation.Plasma prekallikrein deficiency causes a prolonged activated partial thromboplastin time in patients.
Description:
The TNF family ligand ectodysplasin A (EDA) and its receptor EDAR are required for proper development of skin appendages such as hair, teeth, and eccrine sweat glands. Loss of function mutations in the Eda gene cause X-linked hypohidrotic ectodermal dysplasia (XLHED), a condition that can be ameliorated in mice and dogs by timely administration of recombinant EDA. The Eda gene on the X chromosome is transcribed as multiple splice variants, only two of which code for the receptor-binding C-terminal TNF homology domain. These two variants code for 391- and 389-amino acid-long proteins called EDA1 and EDA2. EDA1 binds EDAR, whereas EDA2 binds to another receptor, XEDAR. The biology of EDA2 and XEDAR is distinct from that of EDA1. Indeed, XEDAR-deficient mice have no obvious ectodermal dysplasia phenotype, whereas mice deficient in EDA, EDAR, or the signalling adaptor protein EDARADD all display virtually indistinguishable ectodermal dysplasia phenotypes, indicating the predominance of the EDA1-EDAR axis in the development of skin-derived appendages.
Description:
Notch signalling pathway regulates many different cell fate decisions in both vertebrate and invertebrate species. There are 5 canonical Notch ligands in mammals: Jagged-1, Jagged-2, DLL1, DLL3 and DLL4. These can bind to the four Notch receptors Notch 1-4. It is important for pattern formation during development such as neurogenesis, angiogenesis or myogenesis and regulates T cell development and stem cell maintenance. Notch signalling is also involved in cellular processes through-out adulthood. Signalling via Notch occurs between neighbouring cells and both the receptor and its ligands are transmembrane proteins.
Description:
MultimericCD40L™ is a high activity construct in which two trimeric CD40 ligands are artificially linked via the collagen domain of ACRP30. This construct very effectively simulates the natural membrane-assisted aggregation of CD40L in vivo. It provides a simple and equally potent alternative to CD40L+enhancer combinations. MultimericCD40L™ has been shown to suppress alum-induced IL-1beta release and caspase-1 activation in a dose-, CD40- and time dependent manner, without affecting BMDM (Bone marrow-derived macrophages) viability. It also effectively suppressed the inflammasome function triggered by NLRP3 activators. The secretion of caspase-1 independent inflammatory mediators has been shown to be unaltered or even enhanced.
Description:
IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9) bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1. IL-36Ra inhibits the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 induced by IL-36 in BMDC and CD4 T cells. Skin and dendritic cells are targets of the IL-36 interleukins leading to a Th1 response. These cytokines may represent potential targets for immune-mediated inflammatory conditions or, alternatively, could be used as adjuvants in vaccination.
Description:
Dipeptidyl peptidase-IV (DPPIV) is also known as adenosine deaminase complexing protein 2, DPPIV or CD26 is antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. The substrates of DPPIV are proline (or alanine)-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides. DPPIV plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. DPPIV plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others. DPPIV also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.
Description:
CD47 is involved in the increase in intracellular calcium concentration that occurs upon cell adhesion to extracellular matrix. The protein is also a receptor for the C-terminal cell-binding domain of thrombospondin, and it may play a role in membrane transport and signal transduction. This protein has broad tissue distribution, and is reduced in expression on Rh erythrocytes.
Description:
MHC class I polypeptide-related sequence A (MICA) belongs to the MHC class I family and MIC subfamily. MICA contains one Ig-like C1-type (immunoglobulin-like) domain. Unlike classical MHC class I molecules, MICA does not form a heterodimer with beta-2-microglobulin. MICA acts as a stress-induced self-antigen that is recognized by gamma delta T-cells. MICA is ligand for the KLRK1/NKG2D receptor. MICA bind to KLRK1 leads to cell lysis.
Description:
Matrix metallopeptidase 9 (MMP-9) is also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. . Structurally, MMP9 maybe be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.
UOM:
1 * 50 µG
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