Analytical Data
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Gene name
PRCP
- Application
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Alternative Names
PRCP；PCP；Lysosomal Pro-X carboxypeptidase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P42785
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Expression Region
46-496aa
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AA Sequence
KNYSV LYFQQKVDHF GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC NNTGFMWDVA EELKAMLVFA EHRYYGESLP FGDNSFKDSR HLNFLTSEQA LADFAELIKH LKRTIPGAEN QPVIAIGGSY GGMLAAWFRM KYPHMVVGAL AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIHRS WDAINRLSNT GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA TSSLGTLGWS YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV RPRPSWITTM YGGKNISSHT NIVFSNGELD PWSGGGVTKD ITDTLVAVTI SEGAHHLDLR TKNALDPMSV LLARSLEVRH MKNWIRDFYD SAGKQH
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PRCP (Prolyl Carboxypeptidase) is an enzyme that plays a crucial role in the regulation of biological processes through the cleavage of specific proteins and peptides. Its primary function involves the inactivation of bioactive peptides, such as angiotensin II and neuropeptides, which are integral to cardiovascular, renal, and neurological functions. Research into PRCP has gained momentum due to its potential implications in various pathological conditions, including hypertension, heart failure, and neurological disorders. The overactivity or dysregulation of PRCP can lead to an imbalance in peptide signaling, contributing to disease progression. Consequently, scientists have pursued the recombinant expression of PRCP to study its structure-function relationships and enzymatic mechanisms. Various expression systems, such as bacterial, yeast, and mammalian cells, have been utilized to produce active PRCP for biochemical assays and therapeutic development. By understanding the enzyme's activity and inhibition, researchers aim to identify novel therapeutic targets and strategies for managing diseases related to dysregulated peptide signaling. Additionally, the study of PRCP not only sheds light on its biological significance but also opens avenues for drug discovery and the development of peptide-based therapies. Overall, PRCP represents a promising area of research with potential implications for enhancing our understanding of peptide biology and addressing important medical challenges.
