Analytical Data
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Gene name
PDIA6
- Application
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Alternative Names
PDIA6;ERP5;P5;TXNDC7;Protein disulfide-isomerase A6
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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
Q15084
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Expression Region
20-440aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MLYSSSDDVI ELTPSNFNRE VIQSDSLWLV EFYAPWCGHC QRLTPEWKKA ATALKDVVKV GAVDADKHHS LGGQYGVQGF PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL SALRQLVKDR LGGRSGGYSS GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP WCGHCKNLEP EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV VAVLPHILDT GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA LGIGGFGYPA MAAINARKMK FALLKGSFSE QGINEFLREL SFGRGSTAPV GGGAFPTIVE REPWDGRDGE LPVEDDIDLS DVELDDLGKD EL
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Molecular Weight
48 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
PDIA6, or Protein Disulfide Isomerase Family A member 6, is an important enzyme that plays a critical role in the formation and rearrangement of disulfide bonds within proteins, which is essential for proper protein folding and stability. Recent studies have highlighted its involvement in various cellular processes, including stress response, apoptosis, and signaling pathways. The overexpression or dysfunction of PDIA6 has been linked to several diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases. Thus, understanding the functional mechanisms of PDIA6 and its interactions with other cellular components is crucial for developing therapeutic strategies. Recombination technologies have enabled the production of PDIA6 as a recombinant protein, allowing researchers to study its properties in detail, investigate its structure-function relationships, and assess its potential as a drug target or biomarker. Ongoing research focuses on elucidating the molecular mechanisms by which PDIA6 contributes to disease progression and exploring its therapeutic potential through the modulation of its activity in pathological conditions. This research not only enhances our understanding of protein disulfide isomerases but also opens new avenues for the treatment and diagnosis of various diseases associated with protein misfolding and oxidative stress.











