Analytical Data
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基因名
PRCP
- Application
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别名
PCP; HUMPCP; Lysosomal Pro-X Carboxypeptidase; Angiotensinase C; Lysosomal carboxypeptidase C; Proline carboxypeptidase
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种属
Mouse
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
Q7TMR0
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表达区间
Gln169~Leu443
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分子量
61kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
