Recombinant Human Carboxypeptidase A2/CPA2 Protein (His Tag)

Specifications

Catalog number

PKSH032169-01

Size / count

10 µg

Dry ice

No

Hazardous

No

Discontinued

No

Background

Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. 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.

Abbreviation

Carboxypeptidase A2; CPA2

Synonyms

CPA2; Carboxypeptidase A2

UniProt

P48052

Accession Number

AAP36067.1

Expression System

HEK293 Cells

Tag

C-His

Sequence

Leu17-Tyr417

Field of Research

Cell biology

Endotoxin

< 1.0 EU per μg of the protein as determined by the LAL method.

Purity

> 95 % as determined by reducing SDS-PAGE.

Bioactivity

Not validated for activity

Reconstitution

Please refer to the printed manual for detailed information.

Shipping Conditions

This product is provided as lyophilized powder which is shipped with ice packs.

Storage Conditions

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Calculated Molecular Weight

45.9 kDa

Observed Molecular Weight

50 kDa

Species

Human