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Mouse Anti-EIF2D Recombinant Antibody (2D10) (V2LY-0425-LY1665)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
2D10
Antibody Isotype
IgG2a, κ
Application
WB, ELISA, IP

Basic Information

Immunogen
Amino acids 485-584 of human Eif2d.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
ELISA1:100-1:1,000
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)

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

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.1 mg/ml
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
eukaryotic translation initiation factor 2D
Entrez Gene ID
1939
UniProt ID
P41214
Research Area
Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits.
Biological Process
Formation of translation preinitiation complex Source: UniProtKB
Intracellular protein transport Source: ProtInc
IRES-dependent viral translational initiation Source: UniProtKB
Ribosome disassembly Source: UniProtKB
Cellular Location
Cytoplasm
More Infomation

Kim, H., Aponte-Diaz, D., Sotoudegan, M. S., Arnold, J. J., & Cameron, C. E. (2022). IRES-independent, eIF2A/eIF2D-dependent translation of the enterovirus genome. bioRxiv.

Xu, J., Du, R., Meng, X., Zhao, W., Kong, L., & Chen, J. (2021). Third-generation sequencing indicated that lncrna could regulate eIF2D to enhance protein translation under heat stress in Populus simonii. Plant Molecular Biology Reporter, 39(1), 240-250.

Young, D. J., Meydan, S., & Guydosh, N. R. (2021). 40S ribosome profiling reveals distinct roles for Tma20/Tma22 (MCT-1/DENR) and Tma64 (eIF2D) in 40S subunit recycling. Nature communications, 12(1), 1-16.

Sonobe, Y., Aburas, J., Krishnan, G., Fleming, A. C., Ghadge, G., Islam, P., ... & Kratsios, P. (2021). A C. elegans model of C9orf72-associated ALS/FTD uncovers a conserved role for eIF2D in RAN translation. Nature communications, 12(1), 1-17.

Vasudevan, D., Neuman, S. D., Yang, A., Lough, L., Brown, B., Bashirullah, A., ... & Ryoo, H. D. (2020). Translational induction of ATF4 during integrated stress response requires noncanonical initiation factors eIF2D and DENR. Nature communications, 11(1), 1-11.

Golob-Schwarzl, N., Puchas, P., Gogg-Kamerer, M., Weichert, W., Göppert, B., & Haybaeck, J. (2020). New pancreatic cancer biomarkers eIF1, eIF2D, eIF3C and eIF6 play a major role in translational control in ductal adenocarcinoma. Anticancer Research, 40(6), 3109-3118.

Makeeva, D. S., Lando, A. S., Anisimova, A., Egorov, A. A., Logacheva, M. D., Penin, A. A., ... & Dmitriev, S. E. (2019). Translatome and transcriptome analysis of TMA20 (MCT-1) and TMA64 (eIF2D) knockout yeast strains. Data in brief, 23, 103701.

Akulich, K. A., Sinitcyn, P. G., Makeeva, D. S., Andreev, D. E., Terenin, I. M., Anisimova, A. S., ... & Dmitriev, S. E. (2019). A novel uORF-based regulatory mechanism controls translation of the human MDM2 and eIF2D mRNAs during stress. Biochimie, 157, 92-101.

González-Almela, E., Williams, H., Sanz, M. A., & Carrasco, L. (2018). The initiation factors eIF2, eIF2A, eIF2D, eIF4A, and eIF4G are not involved in translation driven by hepatitis C virus IRES in human cells. Frontiers in microbiology, 9, 207.

Young, D. J., Makeeva, D. S., Zhang, F., Anisimova, A. S., Stolboushkina, E. A., Ghobakhlou, F., ... & Guydosh, N. R. (2018). Tma64/eIF2D, Tma20/MCT-1, and Tma22/DENR recycle post-termination 40S subunits in vivo. Molecular cell, 71(5), 761-774.

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

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