| Description | Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). HRG1-β1 (heregulin-β1, also referred to as NRG1-β1) contains an Ig (immunoglobulin) domain and an EGF (epidermal growth factor)-Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). HRG1-β1 (heregulin-β1, also referred to as NRG1-β1) contains an Ig (immunoglobulin) domain and an EGF (epidermal growth factor)-like domain that is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. The gene HRG1-β1 is mapped to human chromosome 8p12. Recombinant human Heregulin-β1 is a 7.5 kDa polypeptide consisting of only the EGF domain of heregulin-β1 (65 amino acid residues).Application:Heregulin beta -1 human has been used to enhance proliferation of human dermal fibroblasts (hDFs).Heregulin-β1 human has been used in the culture medium for the maintenance of Schwann cells. It has been used to study P-Rex1 (PI(3,4,5)P3-dependent Rac exchanger 1)-driven fibroblast invasiveness... Read More | Apatinib(YN-968D1) is an orally bioavailable, selective VEGFR2 inhibitor with IC50 of 1 nM | Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionPromotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionPromotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CYR61-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3.Banckground:Cyr61, also known as CCN1, is a 40-45 kDa matricellular glycoprotein that plays an important role in cellular adhesion and migration (1). Cyr61 consists of an IGFBP domain, a VWF type C domain, a TSP type I domain, and a cysteine knot domain (2). Mature human Cyr61 shares 93% amino acid sequence identity with mouse and rat Cyr61. It is widely expressed during development and in adult tissues (2, 3). Cyr61 associates with the extracellular matrix (ECM) and with many cell surface molecules including Integrins alpha V beta 3, alpha V beta 5, alpha M beta 2, and alpha 6 beta 1, Syndecan-4, and heparan sulfate proteoglycans (1, 3). Cyr61 mediates the adhesion and migration of multiple cell types and also promotes vascular endothelial cell tubule formation (4-6). Plasmin cleavage of ECM-bound Cyr61 releases a 28 kDa N-terminal fragment which retains the ability to promote endothelial cell migration (7). Cyr61 exhibits both tumorigenic and tumor suppressor properties. It is up-regulated and promotes tumorigenesis, angiogenesis, and metastasis in breast, renal, gastric, squamous cell, and colorectal carcinomas as well as in glioma (8-12). In contrast, whendown-regulated, it suppresses tumor growth in endometrial, hepatic, and non-small cell lung cancers (8, 13, 14). Cyr61 is also up-regulated in injured skin and bone where it induces the expression of growth factors, cytokines, proteases, and integrins involved in wound repair (15, 16)... Read More | Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Currently, the Fn is purified from the plasma, which however is limited by the availability of supply. The the recombinant human fibronectin (OsrhFN) was expressed in the rice endosperm platform, which is animal component free and has high purity, and has been demonstrated has the same physical and chemical with the plasma derived Fn. OsrhFN provides a safety solution to replace the plasma derived FN.pH value: 6.0-8.0... Read More | Inquire |