Recombinant Human Carboxypeptidase A Protein (His Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0564

Recombinant Human Carboxypeptidase A Protein (His Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0564
Catalog No.: BLPSN-0564
Product Overview
Tag | His |
Host Species | Human |
Accession | NP_001859.1 |
Synonym | CPA |
Background | 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. |
Description | A DNA sequence encoding the human CPA1 precursor (NP_001859.1) (Met 1-Tyr 419) was expressed with a C-terminal His tag. |
Source | HEK293 |
Predicted N Terminal | Lys 17 |
AA Sequence | Met 1-Tyr 419 |
Molecular Weight | The secreted recombinant human CPA1 (pro form) consists of 414 a.a. and has a predicted molecular mass of 47 kDa. In SDS-PAGE under reducing conditions, it migrates with the apparent molecular mass of 43 kDa. |
Purity | >97% as determined by SDS-PAGE |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
Bioactivity | Measured by its ability to cleave the colorimetric peptide substrate Ac-Phe-Thiaphe-OH in the presence of 5,5'Dithiobis (2-nitrobenzoic acid) (DTNB). The specific activity is >3,500 pmoles/min/ug. |
Formulation | Lyophilized from sterile PBS, pH 7.4. |
Stability | The recombinant proteins are stable for up to 1 year from date of receipt at -70°C. |
Usage | For Research Use Only |
Storage | Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |