| Description | (D-Trp12,Tyr34)-pTH (7-34) amide (bovine) is a potent and competitive antagonist of parathyroid hormone (PTH), with a K i of 69 nM in bovine renal cortical membrane. (D-Trp12,Tyr34)-pTH (7-34) amide (bovine) can be used for growth and development regulationIn Vitro(D-Trp12,Tyr34)-pTH (7-34) amide (0(D-Trp12,Tyr34)-pTH (7-34) amide (bovine) is a potent and competitive antagonist of parathyroid hormone (PTH), with a K i of 69 nM in bovine renal cortical membrane. (D-Trp12,Tyr34)-pTH (7-34) amide (bovine) can be used for growth and development regulationIn Vitro(D-Trp12,Tyr34)-pTH (7-34) amide (0.05-10 µM) causes a concentration-dependent inhibition of PTHrP or PTH-stimulated cAMP formation in opossum kidney (OK) cells. (D-Trp12,Tyr34)-pTH (7-34) amide (0.1-10 µM) attenuates inhibition of Nap i T promoted by 1 nM of either PTHrP or PTH. MCE has not independently confirmed the accuracy of these methods. They are for reference only.In Vivo(D-Trp12,Tyr34)-pTH (7-34) amide (1 mg/mL once, 0.1 mg/mL for 6 h; i.v.) has no significant effect on serum calcium levels in hypercalcemic athymic nude mice bearing a human squamous cell carcinoma of the lung. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:Ki: 69 nM (PTH)... Read More | DescriptionApolipoprotein E (ApoE) is present in the brain and is mainly produced by astrocytes. It is a 299 amino acid glycoprotein of 34kDa. It is present in all classes of lipoproteins except LDL (low-density lipoprotein). APOE gene has three alleles, such as APOE ε3, APOE ε4and APOE &#DescriptionApolipoprotein E (ApoE) is present in the brain and is mainly produced by astrocytes. It is a 299 amino acid glycoprotein of 34kDa. It is present in all classes of lipoproteins except LDL (low-density lipoprotein). APOE gene has three alleles, such as APOE ε3, APOE ε4and APOE ε2. It is located on human chromosome 19q13.Preparation instructionsFormLyophillized from a 0.2 µm filtered solution in 20 mM sodium phosphate, pH 7.8.Principle... Read More | 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:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, respectively, with MCP-1. CCL7 also shares 58% amino acid identity with MCP-2. CCL7 cDNA encodes a 99 amino acid residue precursor protein from which the N-terminal 23 amino acid residues are cleaved to generate the 76 amino acid residue mature CCL7. Mature CCL7 contains a potential N-linked and several possible O-linked glycosylation sites. Similarly to other C-C chemokines, all three MCP proteins are monocyte chemoattractants. In addition, the three MCPs can chemoattract activated NK cells as well as CD4+ and CD8+ T lymphocytes. All three cytokines have also been shown to attract eosinophils and induce histamine secretion from basophils... Read More | Inquire |