| Description | FANCC Human Pre-designed siRNA Set A contains three designed siRNAs for FANCC gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components FANCC siRNA-1: 5 nmol (HPLC) FANCC siRNA-2: 5 nmol (HPLC) FANCC siRNA-3: 5 nmol (HPLC) siRNA Negative Control:FANCC Human Pre-designed siRNA Set A contains three designed siRNAs for FANCC gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components FANCC siRNA-1: 5 nmol (HPLC) FANCC siRNA-2: 5 nmol (HPLC) FANCC 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 | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin,chymotrypsin,kallikrein and plasmin.Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin,protease complexes and dissociating at pH >10 or <3. Effective Aprotinin is a competitive serine protease inhibitor that inhibits trypsin,chymotrypsin,kallikrein and plasmin.Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin,protease complexes and dissociating at pH >10 or <3. Effective concentration is equimolar with protease.Recombinant aprotinin is expressed in E. Coli, and purified with HPLC. It contains no animal-derived components. This is a recombinant form of bovine lung aprotinin, which is traditionally isolated from bovine lung by methods involving fractional precipitation, gel filtration, and ion exchange chromatography. UNIT DEFINITION:A conversion factor for Aprotinin is: 1 EPU = 1 USP Aprotinin Unit = 1800 KIU... Read More | Purity>95% (SDS-PAGE&HPLC) Endotoxin level<0.1 EU/µgFunctionMay regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn Purity>95% (SDS-PAGE&HPLC) Endotoxin level<0.1 EU/µgFunctionMay regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.Gal-1 is also engaged in many protein-protein interactions. Gal-1 plays a number of crucial roles in neuronal cell differentiation and survival in both the central and the peripheral nervous systems, and the establishment and maintenance of T-cell tolerance and homeostasis in vivo... Read More | 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 member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |