|Place of Origin:||Xuhui, Shanghai, China|
|Certification:||NSF ISO 9001:2015|
|Minimum Order Quantity:||100ug|
|Packaging Details:||ice packaging, carton|
|Delivery Time:||7 days|
|Supply Ability:||1000g per week|
|Source:||E. Coli||Purified By:||HPLC|
|Physical Form:||Lyophilized Powder||Specific Activity:||>4500 USP Units/mg Pro|
|Purity:||One Single Main Band At 24kD By SDS-PAGE||Contaminant Activity:||No Chymotrypsin, Carboxypeptidase A, Or Other Protease Contaminant.|
Sequencing Grade Trypsin, Purified by HPLC, Expressed in E.coli
Sequencing Grade Trypsin
Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Recombinant trypsin is free of any other proteases activities, and TPCK is unnecessary and not contained. Unmodified trypsin is subject to auto-proteolysis, generating fragments that can interfere with protein sequencing or HPLC/MS peptides analysis. YaxinBio’s sequencing grade modified trypsin is recombinant porcine trypsin modified by reductive methylation, rendering it resistant to proteolytic digestion.
Liquid in 50mM HAc, or fluffy solid.
0.5mg/ml in 50mM HAc
≥99% by HPLC
Recombinant porcine trypsin.
No any other proteases activities contaminant.
Unit Definition:One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.2ml at pH7.6 and 25℃, with BAEE as a substrate (1cm light path).
STABILITY OF STORAGE AND TRANSPORT
Stability of storage: Sequencing grade trypsin lyophilized should be stored under 2-8℃ in sealed container.
It is stable within 24 months.After dissolved with 1mM HCl or 50mM HAC, it should be stored under -20℃.
It is no activity loss after 5 times repeated freezing and thawing.
Stability of transport: The product is stable by blue ice insulation transport.
Following reconstitution in 10 mM HCl, Trypsin, recombinant, proteomics grade is stable at -15 to -25 °C for up to one month. After first reconstitution the product must be stored in appropriate aliquots to avoid repeated freezing and thawing.
Serine endopeptidase, hydrolyzing specifically proteins and peptides at the carboxy side of the basic amino acids Arg and Lys. Amide and ester bonds of Arg and Lys are also cleaved.
Contact Person: Miss Eland