Recombinant Human Carboxypeptidase A1/CPA1
| 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
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| 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. | 


 


 
              








