The secreted recombinant pro form of mouse CPA1 comprises 414 amino acids and has a calculated molecular mass of 47 kDa. The recombinant protein migrates as an approximately 42 kDa band in SDS-PAGE under reducing conditions.
Lyophilized from sterile 20mM Tris, 150mM NaCl, pH 7.5 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
安定性 & 保存条件
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Carboxypeptidase A Protein, Mouse, Recombinant (His Tag): 画像
Carboxypeptidase A Protein, Mouse, Recombinant (His Tag): 別名
0910001L12Rik Protein, Mouse; Cpa Protein, Mouse
Carboxypeptidase A 背景情報
Carboxypeptidase A1 （CPA1）is secreted as a pancreatic procarboxypeptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated.
carboxypeptidase A1 (pancreatic)
Catasus, L. et al., 1992, Biochem. J. 287: 299-303.
Moulard, M. et al., 1990, FEBS. Lett. 261: 179-183.