Analytical Data
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Gene name
PDIA3
- Application
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Alternative Names
PDIA3;ERP57;ERP60;GRP58;Protein disulfide-isomerase A3
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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
P30101
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Expression Region
25-505aa
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AA Sequence
SDVLELTDDNFESRISDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASIVGFFDDSFSEAHSEFLKAASNLRDNYRFAHTNVESLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL
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Molecular Weight
59.3 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
PDIA3 (Protein Disulfide Isomerase Family A Member 3) is a pivotal enzyme involved in protein folding, isomerization, and quality control within the endoplasmic reticulum. Its primary function is to catalyze the formation and isomerization of disulfide bonds in nascent polypeptides, which is essential for the proper folding of many proteins. Dysregulation of PDIA3 has been implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, making it a significant target for therapeutic intervention. Recent research has focused on the reconstitution of PDIA3 as a recombinant protein to elucidate its structural and functional properties, thereby providing insights into its role in cellular stress responses and its interactions with other molecules. Understanding the mechanistic details of PDIA3's activity through advanced techniques such as X-ray crystallography and nuclear magnetic resonance can shed light on its potential as a drug target and its involvement in pathological conditions. By generating PDIA3 in a recombinant form, researchers aim to explore its enzymatic capabilities, assess the impact of various post-translational modifications, and investigate potential inhibitors that could modulate its activity in disease contexts. This body of work not only enhances our fundamental understanding of protein folding mechanisms but also opens avenues for therapeutic strategies aimed at restoring the function of misfolded proteins in various diseases. As research progresses, the implications of PDIA3's activity on overall cellular homeostasis and its therapeutic potential become increasingly important, highlighting the protein's relevance in both basic and applied biomedical science.
