Analytical Data
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Gene name
PRCP
- Application
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Alternative Names
PCP; HUMPCP; Lysosomal Pro-X Carboxypeptidase; Angiotensinase C; Lysosomal carboxypeptidase C; Proline carboxypeptidase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P42785
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Expression Region
Asp108~Val376
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Molecular Weight
34kDa
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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 (Prolylcarboxypeptidase) is a serine peptidase that plays a critical role in the regulation of bioactive peptides, particularly in the renin-angiotensin system, which is vital for blood pressure and fluid balance. Research into PRCP has gained prominence due to its involvement in various physiological processes and its potential implications in cardiovascular diseases, hypertension, and metabolic disorders. The enzyme functions by cleaving proline residues from the C-terminus of peptides, influencing their receptor activation and subsequent physiological responses. Understanding PRCP's structure and function can provide insights into its role in disease pathophysiology and therapeutic targets. Recent studies have focused on recombinant expression of PRCP to investigate its enzymatic activity, interaction with peptide substrates, and crystal structure, thereby elucidating its mechanism of action. This research aims to explore the therapeutic potential of PRCP inhibitors or activators as novel strategies for treating conditions associated with dysregulated peptide signaling, highlighting the importance of PRCP in both basic and clinical research settings.
