Trypsin Protein, Pig (P.pastoris, His)

Trypsin is a digestive endopeptidase that catalyzes the hydrolysis of peptide bonds on the carboxyl side of lysine or arginine residues. Trypsin is synthesized in the acinar cells of the pancreas. Trypsin is converted to the active enzyme in the gut. Trypsin Protein, Pig (P.pastoris, His) is the recombinant pig-derived Trypsin protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of Trypsin Protein, Pig (P.pastoris, His) is 223 a.a., with molecular weight of ~25.5 kDa.

Trypsin is a digestive endopeptidase that catalyzes the hydrolysis of peptide bonds on the carboxyl side of lysine or arginine residues. Trypsin is synthesized in the acinar cells of the pancreas as an inactive precursor, trypsinogen. Trypsin is converted to the active enzyme in the gut by the highly specific protease enterokinase. Trypsin in turn activates its own zymogen as well as the other pancreatic zymogens once activated. Trypsin plays pivotal roles in food digestion as well as in cellular signal transduction mediated through proteolytic activation of PARs^[1][2].

Pig

P. pastoris

N-6*His

P00761 (I9-N231)

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IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN

Approximately 25.5 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.