| Description | GRIA2 Human Pre-designed siRNA Set A contains three designed siRNAs for GRIA2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components GRIA2 siRNA-1: 5 nmol (HPLC) GRIA2 siRNA-2: 5 nmol (HPLC) GRIA2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:GRIA2 Human Pre-designed siRNA Set A contains three designed siRNAs for GRIA2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components GRIA2 siRNA-1: 5 nmol (HPLC) GRIA2 siRNA-2: 5 nmol (HPLC) GRIA2 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 | Crude collagenase preparations contain several isoforms of two different collagenases, a sulfhydryl protease, clostripain, a trypsin-like enzyme, and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective at breaking down intercellular matrices, the essential Crude collagenase preparations contain several isoforms of two different collagenases, a sulfhydryl protease, clostripain, a trypsin-like enzyme, and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective at breaking down intercellular matrices, the essential part of tissue dissociation. One component of the complex is a hydrolytic enzyme which degrades the helical regions in native collagen preferentially at the Y-Gly bond in the sequence Pro-Y-Gly-Pro, where Y is most frequently a neutral amino acid. This cleavage yields products susceptible to further peptidase digestion. Crude collagenase is inhibited by metal chelating agents such as cysteine, EDTA or o-phenanthroline but not DFP. It is also inhibited by α2-macroglobulin, a large plasma glycoprotein. Ca2+ is required for enzyme activity. Particular enzymatic profiles of each collagenase have been correlated with the tissues from which the cells for study were obtained (or with the uses to which the cells are put) and as a result of the correlations several types of crude collagenases have been established by Aladdin: Types 1, 2, 3, and 4.This collagenase has been tested with cell lines to verify the product is not cytotoxic. Collagenase is typically used to digest the connective components in tissue samples to liberate individual cells. The concentration for cartilage dispersal is 1-2 mg/ml, but literature searches should be performed for species specific and/or tissue specific concentrations... Read More | Gly-Pro-pNA hydrochloride is a dipeptidyl peptidase inhibitor that inhibits dipeptidyl peptidase II, dipeptidyl peptidase IV and dipeptidyl peptidase IX | Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the receptor XCR1, formally known as GPR5. The expression of lymphotactin is abundant in some activated T cells such as activated CD8+ T cells and other class I MHC restricted T cells. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. XCL1 induces its chemotactic function by binding to a chemokine receptor called XCR1. Recombinant Human XCL1 which is a single non-glycosylated polypeptide chains containing 92 amino acids and it shares approximately 60 % amino acid sequence homology with the murine and rat protein... Read More | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |