Analytical Data
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Gene name
ERP27
- Application
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Alternative Names
PDIA8; C12orf46; Protein Disulfide Isomerase Family A,Member 8
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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 90% as determined by SDS-PAGE.
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Uniprot
Q96DN0
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Expression Region
Glu26~Leu273
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Molecular Weight
32kDa
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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
The ERP27 protein, a member of the family of endoplasmic reticulum (ER) chaperones, plays a significant role in protein folding and quality control within the ER. Its importance has been underscored by research linking it to various cellular processes, including stress responses and the maintenance of proteostasis. ERP27 acts as a critical facilitator in the proper assembly of glycoproteins, thereby influencing the secretion efficiency of proteins and impacting overall cellular function. Furthermore, abnormalities in its expression and function have been associated with several diseases, including cancer and neurodegenerative disorders. Understanding the molecular mechanisms governing ERP27’s role in protein handling and its interaction with misfolded proteins is essential, as it may offer insights into therapeutic targets for disorders stemming from protein misfolding and accumulation. Recent studies have utilized advanced techniques to characterize ERP27's structure and functionality, emphasizing its potential as a biomarker for disease progression and response to treatments. The ongoing exploration of ERP27 not only sheds light on fundamental cellular mechanisms but also opens avenues for novel interventions in disease management through targeted modulation of its activity.
