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Conditions of optimal CPA1 Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
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Introduction
Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. 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.
BP001623-C592: Recombinant Human Carboxypeptidase A1 (CPA1) Enzyme
Source: HEK 293-derived.
Recombinant Human Carboxypeptidase A1 (CPA1) Enzyme is expressed with sequence (Ala111-Tyr419) of Human CPA1 fused with a polyhistidine tag at the C-terminus.
Purity: > 95% by SEC-HPLC and reducing SDS-PAGE.
Endotoxin: < 0.1 ng/ug (1 IEU/ug).
Formulation: 0.2 um filtered solution of 20 mM Tris-HCl, 150 mm NaCl, pH 7.5.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
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