Analytical Data
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Gene name
PDI
- Application
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Alternative Names
PDI；ERBA2L；PDI；PDIA1；Protein disulfide-isomerase
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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
P07237
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Expression Region
18-508aa
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AA Sequence
DAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
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Molecular Weight
57.3kDa
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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
Protein disulfide isomerase (PDI) is a crucial enzyme involved in the formation and isomerization of disulfide bonds within nascent polypeptides in the endoplasmic reticulum (ER). This process is vital for proper protein folding and stability, influencing various cellular functions. Dysregulation of PDI has been implicated in numerous diseases, including neurodegenerative disorders, cancer, and diabetes, making it an important target for therapeutic interventions. Research on PDI has garnered attention due to its dual role as a chaperone, facilitating efficient protein folding, and as a catalyst, promoting the rearrangement of disulfide bonds. Additionally, PDI's involvement in oxidative stress response and its potential interactions with various signaling pathways further underscore its significance in cellular biology. The structure-function relationship of PDI has been extensively studied, revealing insights into its active site mechanisms and the conformational changes that occur during its interaction with substrate proteins. Advances in recombinant protein technology have enabled the production of PDI variants for in-depth functional analyses and the exploration of its therapeutic potential. Overall, the ongoing research on PDI not only enhances our understanding of fundamental biological processes but also opens avenues for the development of novel diagnostic and therapeutic strategies.
