CPA1 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00474 Copy Product Info

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.

CPA1 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00474

Copy Product Info

Pack Size	Price	USA Stock	Global Stock
5 μg	$112	7-10 days	7-10 days
10 μg	$183	7-10 days	7-10 days
20 μg	$292	7-10 days	7-10 days
50 μg	$545	7-10 days	7-10 days
100 μg	$792	7-10 days	7-10 days
200 μg	$1,150	7-10 days	7-10 days
500 μg	$1,900	7-10 days	7-10 days
1 mg	$2,730	7-10 days	7-10 days

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For In stock only · Estimated delivery:USA Stock (1-2 days) Global Stock (5-7 days)

For research use only—not for human use. No sales to individuals. Use as intended only.

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Biological Activity	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description	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.
Species	Human
Expression System	HEK293 Cells
Tag	C-6xHis
Accession Number	AAH05279.1
Synonyms	CPA1,CPA,Carboxypeptidase A1
Amino Acid	Lys17-Tyr419
Construction	Lys17-Tyr419
Molecular Weight	44 KDa (reducing condition)
Endotoxin	< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation	Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 150mm NaCl, pH 7.5.
Stability & Storage	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	Proteins are shipped with blue ice.
Research Background	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.