Analytical Data
-
Gene name
EMC8
- Application
-
Alternative Names
EMC8;C16orf2;C16orf4;COX4AL;ER membrane Protein complex subunit 8
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43402
-
Expression Region
1-210aa
-
AA Sequence
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
EMC8, or the Eight Transmembrane Domain Protein, is a member of the EMC (Endoplasmic Membrane Complex) family, which is critical for the biogenesis and membrane insertion of multi-spanning membrane proteins. Research on EMC8, particularly its functions, structural characteristics, and interactions within the endoplasmic reticulum (ER), has gained significant traction due to its role in protein folding and quality control mechanisms within the cell. Studies have indicated that EMC8 is essential for maintaining proper membrane protein homeostasis and plays a crucial role in regulating cellular responses to stress. Its involvement in various disease states, including neurodegenerative disorders and cancer, has further heightened interest in elucidating its molecular mechanisms and potential therapeutic targets. Recent advances in techniques such as cryo-electron microscopy and high-throughput screening have facilitated a more detailed understanding of EMC8's structure-function relationships, paving the way for potential biomedical applications. Consequently, investigating EMC8 and its reconstitution as a recombinant protein presents an opportunity to not only analyze its biochemical properties but also to explore its role in the broader context of membrane protein biology and disease mechanisms.











