Analytical Data
-
Gene name
EIF3M
- Application
-
Alternative Names
Short name: eIF3m Alternative name(s): Fetal lung protein B5 Short name: hFL-B5 PCI domain-containing protein 1
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q7L2H7
-
Expression Region
2-374aa
-
Molecular Weight
58.4 kDa
-
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
EIF3M, or Eukaryotic Translation Initiation Factor 3 Subunit M, is a vital component of the eukaryotic translation initiation complex and plays a crucial role in the regulation of protein synthesis. Research into EIF3M has gained prominence due to its involvement in various cellular processes, including cell growth, differentiation, and response to stress. Alterations in EIF3M expression levels have been associated with several diseases, particularly cancer, where it may affect tumor progression and metastasis by influencing the translation of specific oncogenes and tumor suppressor genes. Understanding the structure and function of recombinant EIF3M protein can provide insights into its mechanistic role in translation initiation and its potential as a therapeutic target. Furthermore, advances in recombinant DNA technology have enabled the production of purified EIF3M, facilitating detailed biochemical and biophysical characterization. Investigating EIF3M's interactions with other translation factors and its contribution to ribosome assembly is crucial for elucidating the complexities of protein synthesis regulation. Overall, the study of EIF3M as a recombinant protein holds significant promise for uncovering its roles in cellular physiology and disease, potentially leading to innovative strategies for diagnosis and treatment.
