EMS0007
Recombinant Trypsin Dimethlyated
Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris
Synonyme(s) :
Dimethylated rTrypsin, Mass Spectrometry Trypsin, Proteomics grade rTrypsin
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About This Item
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.26
Produits recommandés
Catégories apparentées
Description générale
Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. Trypsin is a pancreatic serine endoprotease which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. The enzyme also exhibits esterase and amidase activities. Trypsin has an average molecular mass of 23.29 kDa and a pH optimum near 8.0.
This product is prepared from recombinant trypsin, porcine sequence and the lysine residues have been dimethylated to further restrict autolysis. It is naturally devoid of chymotryptic activity. This high quality trypsin is suitable for proteomics use.
Specific activity: >= 10,000 BAEE units per mg protein.
This product is prepared from recombinant trypsin, porcine sequence and the lysine residues have been dimethylated to further restrict autolysis. It is naturally devoid of chymotryptic activity. This high quality trypsin is suitable for proteomics use.
Specific activity: >= 10,000 BAEE units per mg protein.
Mention d'avertissement
Danger
Mentions de danger
Classification des risques
Aquatic Chronic 2 - Eye Dam. 1 - Met. Corr. 1 - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3
Organes cibles
Respiratory system
Risques supp
Code de la classe de stockage
8A - Combustible corrosive hazardous materials
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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