| Description | IDO2 Human Pre-designed siRNA Set A contains three designed siRNAs for IDO2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components IDO2 siRNA-1: 5 nmol (HPLC) IDO2 siRNA-2: 5 nmol (HPLC) IDO2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 IDO2 Human Pre-designed siRNA Set A contains three designed siRNAs for IDO2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components IDO2 siRNA-1: 5 nmol (HPLC) IDO2 siRNA-2: 5 nmol (HPLC) IDO2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | 6-Bromo-2-naphthyl β-D-glucuronide is a histochemical substrate for β-D-glucuronidase | Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Receptor-1, PAR-1 Agonist induces activation of protein kinase C isoenzymes alpha and epsilon in human HT-29 colon carcinoma cells expressing PAR1 endogeneously. On the cellular level, Protease-Activated Receptor-1, PAR-1 Agonist and thrombin prompted HT-29 cell migration and matrix adhesion by a PKCepsilon-dependent mechanism as concluded because of the inhibition of PAR1-mediated effects by the PKC inhibitor bisindolylmaleimide I and the PKCepsilon translocation inhibitory peptide EAVSLKPT but not by the PKC inhibitor Gö 6976. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:PAR-1... 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: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively... Read More |