Analytical Data
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Gene name
PDXP
- Application
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Alternative Names
BARGIN;Bargin
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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
Q96GD0
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Expression Region
1-296aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMARCERLRGAALRDVLGRAQGVLFDCDGVL WNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGL RAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLA GDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDP WHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDP ARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVP HYYVESIADLTEGLED
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Molecular Weight
34 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
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Protein Description
The study of PDXP (Peptidyl-Dipeptidase X) recombinant proteins has garnered significant interest due to their potential implications in various biological and medical fields. PDXP, a member of the peptidase family, is involved in protein catabolism and cellular regulation. Its ability to hydrolyze dipeptides and its role in the metabolism of bioactive peptides make it a crucial player in numerous physiological processes, including neurotransmitter regulation and immune responses. Moreover, PDXP's involvement in certain pathologies has prompted researchers to explore its function in diseases such as cancer and neurodegenerative disorders, where altered peptide metabolism may contribute to disease progression. Utilizing recombinant DNA technology, scientists can express and purify PDXP to study its enzymatic properties, substrate specificity, and potential therapeutic applications. By generating recombinant PDXP in various expression systems, researchers can investigate its structure-function relationships, aimed at identifying inhibitors or modulators that could serve as novel drug candidates. This research is further bolstered by advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, providing detailed insights into PDXP's active sites and enzymatic mechanisms. The growing understanding of PDXP's role in cellular processes and its application in biotechnology and pharmacology underscores the importance of this research area, holding promise for developing targeted therapies and enhancing our knowledge of peptide metabolism.
