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Recombinant Human Carboxypeptidase B1/CPB1 Protein (His Tag)

Uniprot : P15086

Cat.No.:PKSH031567
Expression host: HEK293 Cells

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50μg

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Description

Synonyms	Carboxypeptidase B;Pancreas-Specific Protein;PASP;CPB1;CPB;PCPB
Species	Human
Expression_host	HEK293 Cells
Sequence	Met 1-Tyr 417
Accession	NP_001862.2
Mol_Mass	47.0 kDa
AP_Mol_Mass	45 kDa
Tag	C-His
Bio_Activity	Measured by its ability to cleave a colorimetric peptide substrate, Hippuryl-Arg, as measured using the wavelength at 254 nm. The specific activity is > 10000 pmoles/min/μg.

Properties

Purity	> 98 % as determined by reducing SDS-PAGE.
Endotoxin level	< 1.0 EU per μg of the protein as determined by the LAL method.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Formulation	Lyophilized from sterile 25mM MES, 0.1 M NaCl, pH 6.5 Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution	Please refer to the printed manual for detailed information.

Background

Carboxypeptidase B1, also well known as pancreatic procarboxypeptidase B (PCPB), is a highly pancreas -specific protein (PASP), and has been identified previously as a serum marker for acute pancreatitis and pancreatic graft rejection. As the prototype for those human exopeptidases that cleave off basic C-terminal residues, CPB1 specifically cleaves the C-terminal Arg and Lys residues with a preference for Arg. The B1 and B2 forms of procarboxypeptidase B differ from each other mainly in isoelectric point.The deduced amino acid sequence of PCPB predicts a 416-amino acid preproenzyme consisting of a 15-aa signal peptide, a 95-aa activation peptide and a 307-aa mature chain. The secreted PCPB zymogen is converted to enzymatically active CPB1 by limited proteolysis by trypsin.

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