Hydrolyzes peptide bonds at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, recombinant, expressed in Pichia pastoris
Sinónimos:
Dimethylated rTrypsin, Mass Spectrometry Trypsin, Proteomics grade rTrypsin
Slide 1 of 1
Iniciar sesión para ver los precios por organización y contrato.
Seleccione un Tamaño
En este momento no podemos mostrarle ni los precios ni la disponibilidad
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.
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
