| Description | Drd2 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Drd2 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Drd2 siRNA-1: 5 nmol (HPLC) Drd2 siRNA-2: 5 nmol (HPLC) Drd2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 Drd2 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Drd2 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Drd2 siRNA-1: 5 nmol (HPLC) Drd2 siRNA-2: 5 nmol (HPLC) Drd2 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 | Inquire | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3）Less than 10ppm of recombinant trypsin... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 kD subunit. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. IL12 has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Recombinant human IL12 protein, fused to His-tag at C-terminus, was expressed in insect cells using baculovirus expression system and purified by using conventional chromatography techniques... Read More | Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by recruiting leukocytes to acute and chronic inflammation sites. Alternatively-spliced forms are known to occur, but the most common form is a type I transmembrane protein with a 674 aa extracellular domain (ECD) that includes seven C2-type immunoglobulin domains, a 22 aa transmembrane segment, and a 19 amino acid (aa) cytoplasmic tail. Within the ECD, human VCAM-1 shares 75% and 76% aa sequence identity with the mouse and rat VCAM-1, respectively. VCAM-1 binds to leukocyte integrins alpha 4 beta 1 (VLA-4) and alpha 4 beta 7. During the inflammatory adhesion mechanism, activated integrins halt rolling leukocytes and attach them firmly to the vascular endothelium. The VCAM-1:VLA-4/ alpha 4 beta 7 interaction is also thought to be involved in the extravasation of white blood cells through the blood vessel wall to sites of inflammation. ELISA techniques have shown that detectable levels of soluble VCAM-1 are present in the biological fluids of apparently normal individuals, but elevated levels of serum VCAM-1 are indicative of future Atrial Fibrillation incident as well as liver disease. Tumor cells use overexpression of VCAM-1 as means of escaping immune surveillance.Post-translational modifications：Sialoglycoprotein.Function:Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation... Read More |