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Carboxypeptidase B Rat

目录号 : GP21461

Carboxypeptidase-B Rat Recombinant

Carboxypeptidase B Rat Chemical Structure

规格 价格 库存 购买数量
5mg
¥840.00
5-10工作日
15mg
¥2,030.00
5-10工作日
50mg
¥6,300.00
5-10工作日

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Sample solution is provided at 25 µL, 10mM.

产品文档

Quality Control & SDS

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产品描述

Recombinant Rat Carboxypeptidase-B is expressed in E.Coli having a Mw of 31kDa is purified by standard chromatography techniques. Recombinant Rat Carboxypeptidase-B is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. Recombinant Carboxypeptidase-B is free from protease inhibitors such as PMSF and EDTA.

Product Data

Purity Greater than 90% as determined by SDS-PAGE. Source Escherichia Coli.
Phycical Appearance Sterile Filtered lyophilized powder. Shipping Condition Shipped at Room temp.
Synonyms Carboxypeptidase B; Cpb1; Cpb.
Solubility It is recommended to reconstitute the lyophilized Rat Carboxypeptidase-B in sterile 18MΩ-cm H2O or 25mM Tris-HCl pH 7.65 not less than 100µg/ml , which can then be further diluted to other aqueous solutions.
Stability Store the lyophilized Carboxypeptidase-B at 4°C . Upon reconstitute the protein should be stored at 4°C for 2 weeks and for future use below -18°C .Please prevent freeze-thaw cycles.
Biological Activity 170 units/mg protein.
Formulation The protein was lyophilized with 100mM NaCl, mannitol and 20mM Tris pH-7.5.

Introduction

Carboxypeptidase B (EC 3.4.17.2) catalyzes hydrolysis of the basic amino acids lysine, arginine and ornithine from the C-terminal end of polypeptides. The Mw was found to be 34.5 kDa, optimun pH-7.9, and pI-6. Carboxypeptidase B is inhibited by arginine, lysine and ornithine. The enzyme is not inhibited by di-isopropylfluorophosphate (DFP), but it is inhibited by metal chelating agents, e.g., EDTA, 1,10-phenanthroline.

Biological Activity

170 units/mg protein.

Stability

Store the lyophilized Carboxypeptidase-B at 4°C . Upon reconstitute the protein should be stored at 4°C for 2 weeks and for future use below -18°C .Please prevent freeze-thaw cycles.