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Recombinant Human Carboxypeptidase A1/CPA1

Recombinant Human Carboxypeptidase A1/CPA1 Recombinant Human Carboxypeptidase A1/CPA1

Instruction Manual!

Product name: Recombinant Human Carboxypeptidase A1/CPA1
Source:Human Cells
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 150mm NaCl, pH 7.5.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source Human Cells
Description Recombinant Human Carboxypeptidase A1 is produced by our Mammalian expression system and the target gene encoding Lys17-Tyr419 is expressed with a 6His tag at the C-terminus.
Names Carboxypeptidase A1, CPA1, CPA
Accession # P15085
Formulation Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 150mm NaCl, pH 7.5.
Shipping The product is shipped on dry ice/ice packs.
Storage Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
KEDFVGHQVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPGSPIDVRVPFPSIQAVKIFLES HGISYETMIEDVQSLLDEEQEQMFAFRSRARSTDTFNYATYHTLEEIYDFLDLLVAENPHLVSKI QIGNTYEGRPIYVLKFSTGGSKRPAIWIDTGIHSREWVTQASGVWFAKKITQDYGQDAAFTAILD TLDIFLEIVTNPDGFAFTHSTNRMWRKTRSHTAGSLCIGVDPNRNWDAGFGLSGASSNPCSETYR GKFANSEVEVKSIVDFVKDHGNIKAFISIHSYSQLLMYPYGYKTEPVPDQDELDQLSKAAVTALA SLYGTKFNYGSIIKAIYQASGSTIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLA LLTIMEHTLNHPYVDHHHHHH
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.

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