Analytical Data
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Gene name
PDIA4
- Application
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Alternative Names
PDI-A4; ERP70; ERP72; Protein Disulfide Isomerase-Associated 4; Endoplasmic reticulum resident protein 70
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P13667
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Expression Region
Phe505~Thr636
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Molecular Weight
17kDa
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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
PDIA4 (Protein Disulfide Isomerase Family A Member 4) is a crucial enzyme that plays a significant role in protein folding and quality control within the endoplasmic reticulum. It is involved in the formation and rearrangement of disulfide bonds, which are essential for the stability and functionality of many extracellular and membrane proteins. Interest in PDIA4 has grown due to its potential implications in various diseases, including cancer, neurodegenerative disorders, and metabolic diseases. Researchers have been exploring the biochemical properties and mechanisms of PDIA4, particularly its role in the cellular stress response and apoptosis. Additionally, the study of PDIA4 recombinant proteins has opened avenues for therapeutic applications, as manipulating its activity could lead to novel strategies for treating diseases associated with protein misfolding. Understanding PDIA4's structure and function not only sheds light on fundamental cellular processes but also holds promise for developing targeted interventions in disease contexts where protein folding and aggregation are disrupted.
