Analytical Data
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Gene name
PGCP
- Application
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Alternative Names
Carboxypeptidase Q. EC:3.4.17.-. Lysosomal dipeptidase. Plasma glutamate carboxypeptidase
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y646
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Expression Region
1-472 aa
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AA Sequence
MKFLIFAFFGGVHLLSLCSGKAICKNGISKRTFEEIKEEIASCGDVAKAIINLAVYGKAQNRSYERLALLVDTVGPRLSGSKNLEKAIQIMYQNLQQDGLEKVHLEPVRIPHWERGEESAVMLEPRIHKIAILGLGSSIGTPPEGITAEVLVVTSFDELQRRASEARGKIVVYNQPYINYSRTVQYRTQGAVEAAKVGALASLIRSVASFSIYSPHTGIQEYQDGVPKIPTACITVEDAEMMSRMASHGIKIVIQLKMGAKTYPDTDSFNTVAEITGSKYPEQVVLVSGHLDSWDVGQGAMDDGGGAFISWEALSLIKDLGLRPKRTLRLVLWTAEEQGGVGAFQYYQLHKVNISNYSLVMESDAGTFLPTGLQFTGSEKARAIMEEVMSLLQPLNITQVLSHGEGTDINFWIQAGVPGASLLDDLYKYFFFHHSHGDTMTVMDPKQMNVAAAVWAVVSYVVADMEEMLPRS
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Molecular Weight
77.44 kDa
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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
PGCP, or prolyl endopeptidase (PEP), is an enzyme that plays a significant role in the degradation of proline-containing peptides, contributing to various physiological processes, including the regulation of blood pressure and neurotransmitter activity. Its ability to cleave proline-rich peptides makes it a target of interest in multiple areas of biomedical research, particularly in studying neurodegenerative diseases, such as Alzheimer's, where peptide accumulation can lead to disease progression. Researchers are increasingly focused on the structural and functional aspects of PGCP, utilizing techniques such as recombinant protein expression to produce and analyze these enzymes. This involves investigations into their enzymatic mechanisms, substrate specificity, and potential inhibitors, which can pave the way for novel therapeutic strategies. Additionally, understanding the role of PGCP in protein folding and cellular stress responses can provide insights into broader biological functions and interactions. Given its critical importance in maintaining physiological homeostasis, the study of PGCP and its related proteins is essential for developing targeted interventions in a range of medicinal applications.
