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>Human EIF-5A / EIF5 Protein (GST Tag)
|Catalog||Size (Price)||Quantity||In Stock||Operation|
Eukaryotic translation initiation factor 5 Protein Datasheet
EIF-5A / EIF5 Protein Price Inquiry ( Available Sizes )
EIF-5A / EIF5 Protein Product Information
A DNA sequence encoding the mature form of human EIF5 (P55010) (Met1-Asp150) was fused with the GST tag at the N-terminus.
EIF-5A / EIF5 Protein QC Testing
|Purity:||> 95 % as determined by SDS-PAGE||SDS-PAGE:
EIF-5A / EIF5 protein
|Endotoxin:||Please contact us for more information.|
|Stability:||Samples are stable for up to twelve months from date of receipt at -70℃|
|Predicted N terminal:||Met|
|Molecular Mass:||The recombinant human EIF5 /GST chimera consists of 384 amino acids and has a predicted molecular mass of 44.1 kDa. It migrates as an approximately 38-43 KDa band in SDS-PAGE under reducing conditions.|
|Formulation:||Lyophilized from sterile PBS, pH7.4.
EIF-5A / EIF5 Protein Usage Guide
|Storage:||Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|Reconstitution:||A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
EIF-5A / EIF5 Protein Related Products & Topics
EIF-5A / EIF5 Protein Description
EIF-5A, also known as EIF5, plays an important role in the assembly of the 43S pre-initiation complex. In this assembly, EIF-5A interacts with eIF1 and eIF3 and binds the eIF2-GTP/Met-tRNA ternary complex along with the 40S ribosome subunit. EIF-5A is also reported to form a complex with eIF2. It is a critical component of the eIF2regulatory complex that inhibits the activity of the guanine-nucleotide exchange factor (GEF) eIF2B. This complex is suggested to serve as a cytoplasmic reservoir for eIF2 that restricts the guanine nucleotide exchange promoted by the eIF2 beta subunit for the initiation of translation.
- Si K. et al., 1996, J Biol Chem. 71 (28): 16934-8.
- Das S. et al., 1998, J Biol Chem. 272 (50): 31712-8.
- Conte MR. et al., 2006, Biochemistry. 45 (14): 4550-8.