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Trypsin Bovine

目录号 : GP24902

Trypsin Bovine Recombinant

Trypsin Bovine Chemical Structure

规格 价格 库存 购买数量
1mg
¥840.00
5-10工作日
10mg
¥2,030.00
5-10工作日
100mg
¥9,800.00
5-10工作日

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Sample solution is provided at 25 µL, 10mM.

Description

Recombinant Bovine Trypsin is free from any animal and human sources. Trypsin Bovine specifically cleaves peptide bonds after basic amino acids such as lysine and arginine.

Product Data

Purity Greater than 90% as determined by SDS-PAGE. Source Corn.
Phycical Appearance Sterile Filtered lyophilized powder. Shipping Condition Shipped at Room temp.
Solubility It is recommended to reconstitute the lyophilized Bovine Trypsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability Store the Bovine Trypsin between 2-8°C , do not freeze.
Biological Activity 4,313 Units/mg.
Formulation The protein was lyophilized without any additives.

Introduction

Trypsin is a serine protease that hydrolyses proteins, it is found in the digestive system of numerous vertebrates. Trypsin is produced as the inactive proenzyme trypsinogen in the pancreas. Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. Trypsin is secreted into the duodenum, where it acts to hydrolyses peptides into amino acids, which is necessary for the uptake of protein in the food even though peptides are smaller than proteins; they are still too big to be absorbed through the lining of the ileum. The optimal operating pH for Trypsins is about 8 and about 37°C temperature. In cystic fibrosis disease there is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. Trypsin is widely used in various biotechnological processes since itбпs available in high quantity in the pancreases, and can be purified rather easily.

Biological Activity

4,313 Units/mg.

Stability

Store the Bovine Trypsin between 2-8°C , do not freeze.

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