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Mouse Anti-EIF4G1 Recombinant Antibody (3A10) (CBMAB-A2545-LY)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
3A10
Antibody Isotype
IgG2b, κ
Application
WB, ELISA

Basic Information

Immunogen
EIF4G1 (NP_886553, 1500 a.a. ~ 1599 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Purity
> 95% Purity determined 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 4 Gamma 1
Introduction
The protein encoded by this gene is a component of the protein complex EIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure, and recruitment of mRNA to the ribosome. Alternative splicing results in five transcript variants encoding four distinct isoforms. [provided by RefSeq]
Entrez Gene ID
Human1981
Mouse208643
Rat287986
UniProt ID
HumanQ04637
MouseQ6NZJ6
RatD4AD15
Alternative Names
DKFZp686A1451; EIF4F; EIF4G; p220
Research Area
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139).
Biological Process
Behavioral fear response Source: Ensembl
Cap-dependent translational initiation Source: ParkinsonsUK-UCL
Cellular macromolecule biosynthetic process Source: ParkinsonsUK-UCL
Cellular response to nutrient levels Source: ParkinsonsUK-UCL
Developmental process Source: ParkinsonsUK-UCL
Energy homeostasis Source: ParkinsonsUK-UCL
Negative regulation of autophagy Source: ParkinsonsUK-UCL
Negative regulation of neuron death Source: ParkinsonsUK-UCL
Negative regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
Positive regulation of cell death Source: ParkinsonsUK-UCL
Positive regulation of cell growth Source: ParkinsonsUK-UCL
Positive regulation of cellular protein metabolic process Source: ParkinsonsUK-UCL
Positive regulation of eukaryotic translation initiation factor 4F complex assembly Source: ParkinsonsUK-UCL
Positive regulation of G1/S transition of mitotic cell cycle Source: ParkinsonsUK-UCL
Positive regulation of miRNA mediated inhibition of translation Source: ParkinsonsUK-UCL
Positive regulation of mRNA cap binding Source: ParkinsonsUK-UCL
Positive regulation of neuron differentiation Source: Ensembl
Positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
Positive regulation of translation in response to endoplasmic reticulum stress Source: UniProtKB
Regulation of cellular response to stress Source: ParkinsonsUK-UCL
Regulation of gene silencing by miRNA Source: ParkinsonsUK-UCL
Regulation of polysome binding Source: ParkinsonsUK-UCL
Regulation of presynapse assembly Source: ParkinsonsUK-UCL
Regulation of translational initiation Source: UniProtKB
Translation Source: ParkinsonsUK-UCL
Translational initiation Source: ParkinsonsUK-UCL
Cellular Location
Stress granule
Involvement in disease
Parkinson disease 18 (PARK18):
An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
PTM
Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1.
Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription.
More Infomation

Zhao, Y., Li, C., Zhang, Y., & Li, Z. (2022). CircTMTC1 contributes to nasopharyngeal carcinoma progression through targeting miR-495-MET-eIF4G1 translational regulation axis. Cell death & disease, 13(3), 1-14.

Cruz, A., & Joseph, S. (2022). Interaction of the Influenza A Virus NS1 Protein with the 5′-m7G-mRNA· eIF4E· eIF4G1 Complex. Biochemistry, 61(14), 1485-1494.

Sehrawat, U., Haimov, O., Weiss, B., Tamarkin-Ben Harush, A., Ashkenazi, S., Plotnikov, A., ... & Dikstein, R. (2022). Inhibitors of eIF4G1–eIF1 uncover its regulatory role of ER/UPR stress-response genes independent of eIF2α-phosphorylation. Proceedings of the National Academy of Sciences, 119(30), e2120339119.

Tseng, Y. T., Sung, Y. C., Liu, C. Y., & Lo, K. Y. (2022). Translation initiation factor eIF4G1 modulates the assembly of PET region in yeast ribosome biogenesis. Journal of Cell Science.

Saini, P., Rudakou, U., Yu, E., Ruskey, J. A., Asayesh, F., Laurent, S. B., ... & Gan-Or, Z. (2021). Association study of DNAJC13, UCHL1, HTRA2, GIGYF2, and EIF4G1 with Parkinson's disease. Neurobiology of Aging, 100, 119-e7.

Del Valle, L., Dai, L., Lin, H. Y., Lin, Z., Chen, J., Post, S. R., & Qin, Z. (2021). Role of EIF4G1 network in non‐small cell lung cancers (NSCLC) cell survival and disease progression. Journal of cellular and molecular medicine, 25(6), 2795-2805.

Trainor, B. M., Ghosh, A., Pestov, D. G., Hellen, C. U., & Shcherbik, N. (2021). A translation enhancer element from black beetle virus engages yeast eIF4G1 to drive cap-independent translation initiation. Scientific reports, 11(1), 1-18.

Jaiswal, P. K., Koul, S., Palanisamy, N., & Koul, H. K. (2019). Eukaryotic Translation Initiation Factor 4 Gamma 1 (EIF4G1): a target for cancer therapeutic intervention?. Cancer cell international, 19(1), 1-14.

Haimov, O., Sehrawat, U., Tamarkin-Ben Harush, A., Bahat, A., Uzonyi, A., Will, A., ... & Dikstein, R. (2018). Dynamic interaction of eukaryotic initiation factor 4G1 (eIF4G1) with eIF4E and eIF1 underlies scanning-dependent and-independent translation. Molecular and cellular biology, 38(18), e00139-18.

Jaiswal, P. K., Koul, S., Shanmugam, P. S., & Koul, H. K. (2018). Eukaryotic Translation Initiation Factor 4 Gamma 1 (eIF4G1) is upregulated during Prostate cancer progression and modulates cell growth and metastasis. Scientific reports, 8(1), 1-12.

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

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