Analytical Data
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Gene name
EMC9
- Application
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Alternative Names
Protein FAM158A
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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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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, considered a crucial component within the endoplasmic reticulum (ER) and associated with protein quality control, has garnered increasing attention in the field of molecular biology and biochemistry. This protein plays a significant role in the assembly, folding, and trafficking of secretory and membrane-bound proteins, making it vital for cellular homeostasis and function. Emerging research has highlighted EMC9's involvement in various diseases, including neurodegenerative disorders and cancer, where disturbances in protein folding and misfolded protein accumulation are prevalent. Additionally, understanding the molecular mechanisms underlying EMC9's interaction with other ER chaperones and its influence on cellular stress responses could provide insights into therapeutic strategies for related pathologies. The reconstitution of EMC9 as a recombinant protein allows for detailed functional studies, structural analysis, and the potential development of innovative treatments aimed at modulating its activity. As research progresses, EMC9 stands out as a promising target for drug discovery and the enhancement of protein homeostasis in various biological contexts.
