Analytical Data
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Gene name
ERP29
- Application
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Alternative Names
ERP29；C12orf8；ERP28；Endoplasmic reticulum resident Protein 29
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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
P30040
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Expression Region
40-251aa
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AA Sequence
PLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLVAEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKVGAIQRWLKGQGVYLGMPGCLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAF
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Molecular Weight
51.0 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
Related Products
Protein Description
ERP29, or Endoplasmic Reticulum Protein 29, is a member of the 29-kDa family of proteins primarily localized in the endoplasmic reticulum (ER) and has garnered attention for its role in protein folding and quality control within the ER. Studies suggest that ERP29 is involved in the maturation of glycoproteins and may play a critical role in cellular stress responses, potentially contributing to pathophysiological conditions such as neurodegenerative diseases and cancer. Researchers have been investigating the structural characteristics of ERP29 through recombinant protein techniques to elucidate its functional mechanisms and interactions with other ER-resident proteins. The reconstitution of ERP29 as a recombinant protein allows for detailed biophysical and biochemical analyses, offering insights into its folding properties, oligomerization states, and stability under various conditions. Moreover, understanding ERP29's role in the ER's protein-processing machinery may provide valuable implications for therapeutic approaches targeting diseases linked to ER stress and misfolded proteins. As research in this area advances, the potential of ERP29 as a biomarker or therapeutic target continues to be a topic of great interest within the scientific community.
