Recombinant Human Lysosomal Pro-X Carboxypeptidase/PRCP (C-6His)
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| Amount : | 50 µg |
| Content : | Supplied as a 0.2 µm filtered solution of 20mM NaAc-HAc,150mM NaCl,10%Glycerol,pH4.5. |
| Storage condition : | Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. |
| AA sequence : | LRPALRALGSLHLPTNPTSLPAVAKNYSVLYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQALADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGALAASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNTGSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQPLPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETATSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGVRPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTISEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQHVDHHHHHH |
Source: Human Cells.
MW :54.5kD.
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. 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.
MW :54.5kD.
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. 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.
Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Lysosome |
| Tissue Specificity: | Highest levels in placenta, lung and liver. Also present in heart, brain, pancreas and kidney. |
| BioGrid: | 111538. 27 interactions. |
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