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Alkaline Protease, Recombinant Enzyme, Porcine Trypsin

Alkaline Protease, Recombinant Enzyme, Porcine Trypsin

  • Alkaline Protease, Recombinant Enzyme, Porcine Trypsin
  • Alkaline Protease, Recombinant Enzyme, Porcine Trypsin
  • Alkaline Protease, Recombinant Enzyme, Porcine Trypsin
  • Alkaline Protease, Recombinant Enzyme, Porcine Trypsin
  • Alkaline Protease, Recombinant Enzyme, Porcine Trypsin
Alkaline Protease, Recombinant Enzyme, Porcine Trypsin
Product Details:
Place of Origin: China, Shanghai
Brand Name: YAXINBIO
Certification: NSF ISO 9001:2015
Model Number: RPT0201
Payment & Shipping Terms:
Minimum Order Quantity: 10mg
Price: 65$/10mg
Packaging Details: ice packaging, carton
Delivery Time: 7 work days after payment
Payment Terms: T/T
Supply Ability: 1000g per week
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Detailed Product Description
Source: E. Coli Purified By: HPLC
Physical Form: White Or White-like Lyophilized Powder Additives: Carbohydrates
Protein Content: 35% ~ 70% Related Product: Recombinant Trypsin Solution
High Light:

porcine trypsin

,

trypsin enzyme

Alkaline Protease, Recombinant Enzyme, Trypsin Trpsin

 

Recombinant Trypsin

 

Description

 

Trypsinogen
Molecular Weight: 24 kDa
Extinction Coefficient: E1% = 14.4 (280 nm)
pI: 9.3

 

Trypsinogen, the proenzyme (zymogen) form of trypsin, is produced in the acinar exocrine cells  of the pancreas. Three isoforms are excreted from the human pancreas. The cationic and anionic  forms are the predominant human isoforms. The inhibitor-resistant mesotrypsinogen is found only  in trace amounts.The proenzyme is activated only after it reaches the lumen of the small intestine. Enterokinase activates pancreatic trypsinogen to trypsin by the hydrolysis of a hexapeptide(for  bovine trypsin at the Lys - Ile peptide bond) from the NH2 terminus. Bovine trypsinogen consists  of a single polypeptide chain of 229 amino acids and is cross linked by six disulfide bridges. Trypsin

can autocatalytically activate more trypsinogen to trypsin. Trypsin consists of a single chain polypeptide  of 223 amino acid residues. This native form of trypsin is refered to as β-trypsin. Autolysis of β-trypsin (which is cleaved at Lys- Ser in the bovine sequence) results in α-trypsin which is held together by disulfide bridges. Trypsin is a member of the serine protease S1 family. The active site amino acid residues of trypsin include His and Ser Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end

of lysine and arginine amino acid residues. The optimum pH of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF and by metal chelating agents, e.g.EDTA.

Recombinant Porcine Trypsin is a genetically engineered protein expressed in E.coli and purified

by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.

 

Main Features

 

Format

White lyophilized

Specific activity

≥3800 USP units/mg pro

Purity(RP-HPLC)

NLT 70% β-trysin, NMT 20% α-trypsin

Contaminant activity

No chymotrypsin, carboxypeptidase A, and other protease contaminant.

 

 

 

 

 

 

 

Unit Definition

 

One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25℃, with BAEE as a substrate (1cm light path).

 

Recommend Usage

 

Prepare 1-10mg/ml recombinant trypsin with 1mM HCl.The ratio to aimed protein is 1:50 to 1:1000 (w/w).The optimum pH is pH7-10.

Alkaline Protease, Recombinant Enzyme, Porcine Trypsin 0

Contact Details
Shanghai Yaxin Biotechnology Co.,Ltd.

Contact Person: Miss Eland

Tel: +8613482039151

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