| Description | Pancreatic lipase,when prepared essentially free of colipase,is strongly inhibited by conjugated bile salts at or above their critical micelleconcentration. The addition of colipase restores activity to the bile-salt-inhibited lipase,and gel filtration experiments indicate that colipase in bile saltPancreatic lipase,when prepared essentially free of colipase,is strongly inhibited by conjugated bile salts at or above their critical micelleconcentration. The addition of colipase restores activity to the bile-salt-inhibited lipase,and gel filtration experiments indicate that colipase in bile salt solution formsa dimer,which createsa 1:1 complex with lipase.PROPERTIESLipase and colipase interact in a stoichiometric relationship, with colipase classified as a co-enzyme for lipase. Colipase is a single-chain polypeptide with a molecular weight of approximately 11,000, containing fivedisulfide bridges and an isoelectric point of 5.0.APPLICATIONUse colipase as a co-emulsifier in diagnostic tests for the determination of lipase activity in combination with a chromogenic lipase substrate.ATTENTIONFor your safety and health, please wear a lab coat and disposable gloves... Read More | 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 | Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionOsteoprotegerin (OPG), also named osteoclastogenesis inhibitory factor (OCIF), and tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), is a TNFRSF11B-encoded protein in humans. Acts as decoy receptor for RANKL and thereby Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionOsteoprotegerin (OPG), also named osteoclastogenesis inhibitory factor (OCIF), and tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), is a TNFRSF11B-encoded protein in humans. Acts as decoy receptor for RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local RANKL/OPG ratio. May also play a role in preventing arterial calcification. May act as decoy receptor for TRAIL and protect against apoptosis. TRAIL binding blocks the inhibition of osteoclastogenesis.OPG has been applied to decrease bone resorption in women with postmenopausal osteoporosis and in patients with lytic bone metastases... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：p53 is well known for its key role as a tumor suppressor protein. It is 393 amino acids (aa) in length with a predicted molecular weight of 44 kDa. It belongs to the p53 family that also includes p63 and p73Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：p53 is well known for its key role as a tumor suppressor protein. It is 393 amino acids (aa) in length with a predicted molecular weight of 44 kDa. It belongs to the p53 family that also includes p63 and p73. Structurally, p53 is characterized by an N-terminal transactivation domain, central DNA-binding and oligomerization domains, and a C-terminal regulatory domain. It is thought to exist as a homotetramer, and it exhibits approximately 72% and 76% aa identity with its mouse and rat orthologs, respectively. Mutations in the p53 gene are one of the most frequent genomic events accompanying oncogenic transformation. p53 responds to signals such as DNA damage or cell stress primarily through its actions as a transcription factor. Among its gene targets are a range factors that promote DNA repair mechanisms or apoptosis, including cell cycle regulatory proteins and members the Bcl-2 family. Because of its critical role in genomic homeostasis, p53 activities are tightly regulated by a network of protein-protein interactions, microRNAs, and a range of post-translational modifications, including phosphorylation, acetylation, methylation, and ubiquitination. A widely studied regulator is Murine Double Minute 2 (MDM2). MDM2 is known to suppress p53 activity through direct binding or through its actions as a Ubiquitin ligase (E3) that catalyzes p53 ubiquitination and proteasome-mediated degradation... Read More | Inquire |