Analytical Data
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Gene name
EMC9
- Application
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Alternative Names
EMC9；C14orf122；FAM158A；ER membrane Protein complex subunit 9
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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
Q9Y3B6
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Expression Region
1-208aa
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AA Sequence
MGEVEISALAYVKMCLHAARYPHAAVNGLFLAPAPRSGECLCLTDCVPLFHSHLALSVMLEVALNQVDVWGAQAGLVVAGYYHANAAVNDQSPGPLALKIAGRIAEFFPDAVLIMLDNQKLVPQPRVPPVIVLENQGLRWVPKDKNLVMWRDWEESRQMVGALLEDRAHQHLVDFDCHLDDIRQDWTNQRLNTQITQWVGPTNGNGNA
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Molecular Weight
39.1 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
The EMC9 protein, a member of the endoplasmic reticulum (ER) membrane complex (EMC), has garnered significant attention due to its critical role in protein translocation and folding within the ER, a vital cellular organelle that ensures proper protein maturation. Research into EMC9 is primarily driven by its implications in various cellular processes, including lipid homeostasis, membrane biogenesis, and the coordination of protein quality control mechanisms. Abnormalities in these functions can lead to a range of diseases, such as neurodegenerative disorders and congenital disorders of glycosylation. Initial studies suggest that EMC9 may interact with key components of the translocon, influencing the trafficking of proteins destined for secretion or membrane insertion. Additionally, evidence indicates that EMC9 may play a role in the regulation of ER stress responses, linking it to the cellular adaptation mechanisms under stress conditions. Investigating EMC9's structure, function, and interactions with other ER-resident proteins is crucial for understanding its overall impact on cellular physiology and its potential as a therapeutic target. Advances in techniques such as cryo-electron microscopy and molecular biology tools are paving the way for deeper insights into the mechanistic roles of EMC9. Consequently, ongoing research aims to elucidate these pathways thoroughly, potentially revealing new avenues for intervention in related diseases and enhancing our understanding of ER dynamics in health and disease.
