Analytical Data
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Gene name
EMC4
- Application
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Alternative Names
Cell proliferation-inducing gene 17 protein (Transmembrane protein 85) (TMEM85)
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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
Q5J8M3
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Expression Region
2-183aa
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Molecular Weight
26.0 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
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Protein Description
EMC4, a member of the endoplasmic reticulum membrane protein complex (EMC), plays a crucial role in the biogenesis of membrane proteins. The EMC complex facilitates the insertion and folding of hydrophobic membrane proteins into the endoplasmic reticulum (ER), which is essential for maintaining cellular homeostasis and facilitating proper signal transduction. Research into EMC4 has gained traction due to its potential implications in various diseases, including neurodegenerative disorders and cancers, where membrane protein misfolding and aggregation can disrupt cellular functions. Recent studies have highlighted the structure and functional dynamics of EMC4, revealing its interactions with different substrates and other molecular chaperones in the ER. Understanding the mechanisms by which EMC4 assists in membrane protein assembly not only enhances our fundamental knowledge of protein biology but also opens avenues for therapeutic interventions targeting diseases associated with protein misfolding. Consequently, EMC4 represents a significant focus for researchers aiming to elucidate the complexities of protein synthesis, folding, and quality control within the cell, ultimately contributing to the development of strategies to combat related pathologies.
