Human Recombinant EIF5 protein, GST Tag (V2LY-0526-LY3825)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
GST Tag
Protein Construction
This product is Human Recombinant EIF5 protein, GST Tag consist of Amino Acid: 1-150 and predicts a molecular mass of 44.1 kDa.
Molecule Mass
44.1 kDa
Sequence
Amino Acid: 1-150
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Eukaryotic Translation Initiation Factor 5
Research Area
Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
Biological Process
Activation of GTPase activity Source: Ensembl
Formation of cytoplasmic translation initiation complex Source: GO_Central
Formation of translation preinitiation complex Source: GO_Central
Regulation of translational initiation Source: CACAO
Cellular Location
Cytosol; Plasma membrane; Cytoplasm

Li, Z., Wu, Y., Fu, Y., Chen, X., Zhao, X., Wu, X., ... & Sun, F. (2022). Cyst stem cell lineage eIF5 non-autonomously prevents testicular germ cell tumor formation via eIF1A/eIF2γ-mediated pre-initiation complex. Stem cell research & therapy, 13(1), 1-18.

Paul, E. E., Lin, K. Y., Gamble, N., Tsai, A. W. L., Swan, S. H., Yang, Y., ... & Marintchev, A. (2022). Dynamic interaction network involving the conserved intrinsically disordered regions in human eIF5. Biophysical Chemistry, 281, 106740.

Singh, C. R., Jaiswal, R., Escalante, C. R., & Asano, K. (2022). Label-free protocol to quantify protein affinity using isothermal titration calorimetry and bio-layer interferometry of a human eIF5-mimic protein. STAR protocols, 3(3), 101615.

Marintchev, A., Paul, E. E., Lin, K. Y., Tsai, A. W. L., Yang, Y., Gamble, N., & Doran, M. (2022). Dynamic Interaction Network Involving the Conserved Intrinsically Disordered Regions in Human eIF5. The FASEB Journal, 36.

Cai, S. X., Chen, W. S., Zeng, W., Cheng, X. F., Lin, M. B., & Wang, J. S. (2021). Roles of HDAC2, eIF5, and eIF6 in lung cancer tumorigenesis. Current medical science, 41(4), 764-769.

Zeman, J., Itoh, Y., Kukačka, Z., Rosůlek, M., Kavan, D., Kouba, T., ... & Valášek, L. S. (2019). Binding of eIF3 in complex with eIF5 and eIF1 to the 40S ribosomal subunit is accompanied by dramatic structural changes. Nucleic acids research, 47(15), 8282-8300.

Lin, K. Y., Nag, N., Pestova, T. V., & Marintchev, A. (2018). Human eIF5 and eIF1A compete for binding to eIF5B. Biochemistry, 57(40), 5910-5920.

Llácer, J. L., Hussain, T., Saini, A. K., Nanda, J. S., Kaur, S., Gordiyenko, Y., ... & Ramakrishnan, V. (2018). Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition. Elife, 7, e39273.

Ross, J. A., Bressler, K. R., & Thakor, N. (2018). Eukaryotic initiation factor 5B (eIF5B) cooperates with eIF1A and eIF5 to facilitate uORF2-mediated repression of ATF4 translation. International journal of molecular sciences, 19(12), 4032.

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For research use only. Not intended for any clinical use.

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