Recombinant Human Lysosomal Pro-X Carboxypeptidase/PRCP

Instruction Manual!

Product name:	Recombinant Human Lysosomal Pro-X Carboxypeptidase/PRCP
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 NaAc-HAc,150mM NaCl,10%Glycerol,pH4.5.
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 Lysosomal Pro-X Carboxypeptidase is produced by our Mammalian expression system and the target gene encoding Leu22-His496 is expressed with a 6His tag at the C-terminus.
Names	Lysosomal Pro-X Carboxypeptidase, Angiotensinase C, Lysosomal Carboxypeptidase C, Proline Carboxypeptidase, Prolylcarboxypeptidase, PRCP, PRCP, PCP
Accession #	P42785
Formulation	Supplied as a 0.2 μm filtered solution of 20mM NaAc-HAc,150mM NaCl,10%Glycerol,pH4.5.
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	LRPALRALGSLHLPTNPTSLPAVAKNYSVLYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSI LFYTGNEGDIIWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQAL ADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGALAASAPIWQFEDLVPCG VFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNTGSGLQWLTGALHLCSPLTSQDIQHLKDWISE TWVNLAMVDYPYASNFLQPLPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNI SETATSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGVRPRPSWITTMY GGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTISEGAHHLDLRTKNALDPMSVLLARSL EVRHMKNWIRDFYDSAGKQHVDHHHHHH
Background	Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.