CPA2 Protein, Human, Recombinant (His)

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.

Pack Size	Availability	Price/USD
10 μg	5 days	$ 184.00
50 μg	5 days	$ 545.00
500 μg	5 days	$ 1,900.00
1 mg	5 days	$ 2,730.00

Pack Size

Availability

Price/USD

Quantity

10 μg

5 days

$ 184.00

50 μg

5 days

$ 545.00

500 μg

5 days

$ 1,900.00

1 mg

5 days

$ 2,730.00

Description

Species	Human
Expression System	Human Cells
Tag	C-6His
Accession Number	AAP36067.1
Synonyms	CPA2, Carboxypeptidase A2
Amino Acid	Leu17-Tyr417
Construction	Recombinant Human Carboxypeptidase A2 is produced by our Mammalian expression system and the target gene encoding Leu17-Tyr417 is expressed with a 6His tag at the C-terminus.
Protein Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight	50 KDa, reducing conditions

Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mm NaCl, pH 7.5.
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Stability & Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Research 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.

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CPA2 Protein, Human, Recombinant (His)

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