Rhesus macaque CD40 / TNFRSF5 Protein, Fc Tag
产品名称: Rhesus macaque CD40 / TNFRSF5 Protein, Fc Tag
英文名称: Rhesus macaque CD40 / TNFRSF5 Protein, Fc Tag
产品编号: CD0-C5259
产品价格: 0
产品产地: USA
品牌商标: ACROBiosystems
更新时间: null
使用范围: null
北京百普赛斯生物科技股份有限公司
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分子量:30 kDa 纯度:>95% as determined by SDS-PAGE. 内毒素:Less than 1.0 EU per μg of the Human Carbonic Anhydrase II, His Tag by the LAL method. Buffer:20 mM Tris, pH 8.0, with 150 mM NaCl, 1 mM DTT. 生物活性:Measured by its esterase activity for digestion of 4NitrophenylAcetate(4NPA). The specific activity is > 150 pmoles/min/μg. 产品特性:Human Carbonic Anhydrase II, His Tag is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 30 kDa. The predicted N-terminus is Ser 2. The reducing (R) protein migrates as 30 kDa in SDS-PAGE . 产品背景:Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes. CAs form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs rather slowly in the absence of a catalyst. One of the functions of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues. The active site of most carbonic anhydrases contains a zinc ion. They are, therefore, classified as metalloenzymes. There are at least five distinct CA families (α, β, γ, δ and ε). These families have no significant amino acid sequence similarity and in most cases are thought to be an example of convergent evolution. The α-CAs are found in humans. Carbonic anhydrase II (CA2) is also known as Carbonate dehydratase II, Carbonic anhydrase C, is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to interact with Band 3 and Sodium-hydrogen antiporter 1.SDS-PAGE