background:

Trypsin belongs to the serine protease family and can specifically cleave the carboxyl groups of lysine and arginine residues in polypeptide chains. Trypsinogen is secreted by the pancreas and is decomposed into activated trypsin by the restriction of enterokinase or trypsin, which is an endopeptidase. It not only acts as a digestive enzyme, but also limits the decomposition of precursors of other enzymes such as chymotrypsinogen, carboxypeptidase, and phospholipase, and plays an activating role. It is the most specific protease.

Rhinogen ® Trypsin (Sequencing Grade) is a recombinant trypsin obtained by recombinant expression in a recombinant E. coli system and purification by multi-step chromatography. The enzyme is methylated and mutated to ensure that it does not self-cleave, thereby removing the pseudo-chymotrypsin activity caused by self-cleavage. The purity of the enzyme is ≥95%, and there is no contamination by chymotrypsin and other proteases. TPCK is not required to inhibit the activity of other enzymes. Its amino acid sequence is homologous to the sequence of porcine trypsin, and its molecular weight is about 25kDa. It can specifically cleave the carboxyl groups of lysine and arginine residues in polypeptide chains.

Packing Specifications:

Rhinogen ® Trypsin (Sequencing Grade) packaging specifications are as follows:

QIP-003 is provided as a lyophilized powder.

Product Source:

Rhinogen ® Trypsin (Sequencing Grade) is a recombinant trypsin produced by recombinant E. coli system and purified by multi-step chromatography. Its amino acid sequence is homologous to porcine trypsin sequence and its molecular weight is about 25kDa.

Product Quality:

SDS-PAGE analysis showed purity ≥95%; no contaminating protease activity was detected.

Product Features:

The optimum pH is 7.0-8.0; specific activity (unit/mg) ≥4500 USP units/mg.

Storage conditions:

1. Use ice packs for transportation. Please place the enzyme at -20℃ immediately after receiving the product and seal it to prevent moisture.

2. After dissolving with 50mM HAc or 1mM HCl, store at -70℃; if stored at 2-8℃ after dissolution, use within 24 hours. Avoid long-term storage at room temperature and avoid repeated freezing and thawing.

Features:

Rhinogen ® Trypsin (Sequencing Grade) is a highly purified and very stable recombinant protease with high stability and high specific activity.

1. High purity: no contaminating protease, purity ≥ 95%;

2. High stability: Each batch of products undergoes strict quality control to achieve batch-to-batch stability ;

3. No self-cleavage: Recombinant methylation-modified mutant trypsin does not self-cleave;

4. No animal origin: Recombinant production, no exogenous virus contamination, and no animal origin raw materials are used in the production process.

application:

1. Peptide spectrum , peptide fingerprint or protein sequence analysis;

2. Proteomic research.

Instructions:

This product is for research use only and is not intended for diagnostic or therapeutic use in humans or animals.