Analytical Data
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Gene name
ERP44
- Application
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Alternative Names
TXNDC4; PDIA10; Thioredoxin Domain Containing 4; Protein Disulfide Isomerase Family A,Member 10
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Species
Mouse
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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
Q9D1Q6
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Expression Region
Met1~Ala322
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Molecular Weight
41kDa
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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
ERP44, or Endoplasmic Reticulum Protein 44, is a key protein within the endoplasmic reticulum (ER) that plays a significant role in cellular protein folding and quality control. As a member of the thioredoxin family, ERP44 functions primarily as an oxidative-reductive protein, facilitating the formation and isomerization of disulfide bonds in nascent polypeptides. The importance of ERP44 has been underscored by its involvement in the management of ER stress and its potential role in various diseases, including neurodegeneration and cancer. Research has increasingly focused on the functional implications of ERP44, particularly its interactions with other chaperones and folding enzymes, as well as its contribution to the unfolded protein response (UPR). Understanding the precise mechanisms of ERP44 has vital implications for developing therapeutic strategies aimed at diseases linked to protein misfolding and ER dysfunction. Advanced techniques in molecular biology and biochemistry continue to unravel the complexities of ERP44 structure and function, paving the way for potential innovations in medical science related to protein homeostasis.
