Analytical Data
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Gene name
PDIA6
- Application
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Alternative Names
PDI-A6; TXNDC7; P5; ERp5; Thioredoxin Domain Containing 7(Protein Disulfide Isomerase); Protein Disulfide Isomerase-Associated 6; Endoplasmic reticulum protein 5
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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
Q15084
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Expression Region
Leu20~Leu440
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Molecular Weight
50kDa
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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
PDIA6 (protein disulfide isomerase family A member 6) is a crucial enzyme involved in the formation and reshaping of disulfide bonds in proteins, playing a significant role in protein folding and maturation within the endoplasmic reticulum. Recent studies have highlighted its potential implications in various diseases, including cancer and neurodegenerative disorders, where improper protein folding may lead to pathological conditions. As a member of the protein disulfide isomerase family, PDIA6 possesses multiple catalytic sites that allow it to not only assist in the proper folding of proteins but also maintain cellular redox homeostasis. Given its importance in the cellular stress response and potential regulatory functions, researchers are increasingly focusing on the structural and functional characterization of PDIA6 to elucidate its mechanisms of action. Additionally, the examination of PDIA6 in the context of specific diseases may provide insights into novel therapeutic strategies, as modulating its activity could influence protein folding dynamics and disease progression. Understanding the roles of PDIA6 in various cellular processes and its interaction with other molecular partners is crucial for revealing its full biological significance, making it a promising target for future research aimed at developing interventions for diseases linked to protein misfolding and cellular dysfunction.
