Analytical Data
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Gene name
PEPD
- Application
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Alternative Names
PEPD;PRD;Xaa-Pro dipeptidase
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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
P12955
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Expression Region
2-493aa
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AA Sequence
AAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGG EETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLP ASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVN TDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKI SSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENS AVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTAD QKAVYEAVLRSSRAVMGAMKPGVWW PDMHRLADRIHLEELAHMGILSGSVDAMVQAHLGAVFMPHGLGHFLGIDV HDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDHLLDEAL ADPARASFFNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIE ACMAGCDKAFTPFSGPK
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Molecular Weight
54 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
PEPD (Prolyl Endopeptidase) is an important serine protease that plays a crucial role in the metabolic degradation of dietary proteins and the regulation of bioactive peptides. Its activity is primarily focused on cleaving proline-containing peptides, which are abundant in various food sources and biologically active molecules. Research into PEPD has gained momentum due to its potential implications in human health, particularly in relation to neurodegenerative diseases, metabolic disorders, and psychiatric conditions. Elevated levels of PEPD are associated with specific disorders, suggesting that it could serve as a therapeutic target or a biomarker for diseases like schizophrenia or Alzheimer's. Furthermore, the enzymatic characterization of PEPD can pave the way for biotechnological applications, such as the development of functional foods or nutraceuticals designed to modulate peptide profiles for health benefits. As a result, the study of PEPD has broadened to encompass molecular biology, biochemistry, and pharmacology, with researchers focusing on the enzyme's structure, function, and interaction with peptides to uncover its potential roles in both health and disease.
