- Category :
Pharmaceuticals and Biochemicals/Biochemicals and biotech products
- CAS NO : 9002-07-7
- EC NO : 232-650-8
- Molecular Formula : C6H15O12P3
- Main Specifications : ug;mg;g
- Synonyms : Trypsin from bovine pancreas;trypsin from hog pancreas;trypsin type ix from porcine pancreas;trypsin type xi dpcc treated from*bovine pancreas;trypsin tpck treated from*bovine pancreas;trypsin type xii-S from bovine pancreas;trypsin-edta solution (1X)*cell culture tested;trypsin-edta solution cell*culture tested;trypsin-edta solution for endothelial*cell cultur;trypsin 1X solution cell culture tested;trypsin 10X solution cell*culture tested;trypsin 1:250 from porcine pancreas*cell culture;trypsin from porcine pancreas cell*culture tested;trypsin from human pancreas;trypsin tablets 1 mg with buffer salts;Trypsin, bovine, USP Grade;Trypsin, Bovine Pancreas;Trypsin, Excision Grade, Bovine Pancreas;Trypsin, Iodination Grade, Human Pancreas;Trypsin, DPCC treated, bovine pancreas;Trypsin porcine pancreas;Trypsin, TPCK treated, bovine pancreas;Recombinant Trypsin,from E.coli;Recombinant Human Trypsin,from E.coli;Sequencing recombinant trypsin,from E.coli;Trypsin TPCK,pancreas basic;Trypsin,recombinant from E.coli;Trrpsin,sequence, recombinant;Trypsin TPCK;Trrpsin,sequence,recombinant;
Package: Aluminum Foil Bag
Uses : Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues.
Product description:
Sequencing Grade Trypsin
Animal Origin Free
CAS: 9002-07-7
EC: 3.4.21.4
SOURCE
Expressed in E.Coli, purified by HPLC.
DESCRIPTION
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 pH optimum 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 Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There is no trace of contaminating enzyme activities such as carboxypeptidases and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparations.
MAIN FEATURES
Source E.Coli
Purified by HPLC
Physical form White or white-like lyophilized powder
Specific activity NLT 4500 USP units/mg pro.
No Contaminant activity No chymotrypsin, carboxypeptidase A, or other proteases contaminant.
APPLICATION
Protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or MS/MS spectral matching. It is suitable for digestion reactions in-solution or in-gel.
RECOMMEND USAGE
To prepare 1-10mg/ml with 1ml 1mM HCl, used within 2 days, or stored below -20℃ after repacked
STORAGE AND STABILITY
Recommend recombinant trypsin lyophilized powder stored under 2-8℃ in sealed container. It is stable within 24 months.
After dissolved, it should be stored under -20℃, no activity lose after 10 times repeated freezing and thawing.
RELATED PRODUCT: Recombinant Trypsin (sequencing purity), Recombinant Carboxypeptidase B (sequencing purity), V8 (sequencing purity), Recombinant Chymotrypsin (sequencing purity)
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