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AB225953

Anti-EIF2G/EIF2S3 antibody

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(2 Publications)

Rabbit Polyclonal EIF2G/EIF2S3 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human EIF2S3 aa 150 to C-terminus.

View Alternative Names

EIF2G, EIF2S3, Eukaryotic translation initiation factor 2 subunit 3, Eukaryotic translation initiation factor 2 subunit gamma X, eIF2-gamma X, eIF2gX

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EIF2G/EIF2S3 antibody (AB225953)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EIF2G/EIF2S3 antibody (AB225953)

Paraffin embedded human pancreatic tissue stained for EIF2G/EIF2S3 with ab225953 (1/100 dilution) in immunohistochemical analysis.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EIF2G/EIF2S3 antibody (AB225953)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-EIF2G/EIF2S3 antibody (AB225953)

Paraffin embedded human tonsil tissue stained for EIF2G/EIF2S3 with ab225953 (1/100 dilution) in immunohistochemical analysis.

Western blot - Anti-EIF2G/EIF2S3 antibody (AB225953)
  • WB

Supplier Data

Western blot - Anti-EIF2G/EIF2S3 antibody (AB225953)

All lanes:

Western blot - Anti-EIF2G/EIF2S3 antibody (ab225953) at 1/1000 dilution

All lanes:

HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate

Secondary

All lanes:

Goat polyclonal to rabbit at 1/100000 dilution

Predicted band size: 51 kDa

true

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human EIF2S3 aa 150 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

P41091

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

EIF2G also known as EIF2S3 is a part of the eukaryotic translation initiation factor 2 (eIF2) complex. It weighs about 52 kDa and plays a role in the initiation of protein synthesis. EIF2G expresses in various tissues with high levels found in the brain and testis. It associates with other subunits EIF2α and EIF2β to form the eIF2 complex which is essential for the binding of the initiator methionyl-tRNA to the ribosome in a GTP-dependent manner.
Biological function summary

EIF2G participates in the regulation of protein synthesis at the translation initiation step. As part of the eIF2 complex it facilitates the delivery of initiator methionyl-tRNA to the ribosome. This complex is critical for ensuring the accurate start of protein translation. EIF2G works closely with GTP and methionyl-tRNA contributing to the assembly of the translation initiation complex. The function of EIF2G also extends to its involvement in cellular response to stress due to its role in protein synthesis.

Pathways

EIF2G plays a central role in the integrated stress response pathway and the general control response. These pathways allow cells to manage stress and amino acid availability. EIF2G operates alongside proteins such as GCN2 and PERK which phosphorylate EIF2α to modulate translation initiation during stress conditions. This regulation supports cell survival under adverse conditions by reducing overall protein synthesis and promoting the translation of specific stress-related proteins.

EIF2G is associated with neurodegenerative diseases and certain cancers. Aberrations in the eIF2-mediated translation initiation can contribute to the pathogenesis of Alzheimer's disease where dysregulated protein synthesis impacts neuron function. In cancer altered EIF2G activity may lead to uncontrolled cell growth due to changes in protein synthesis patterns. Connections exist between EIF2G and other translational factors such as mTOR which further underline its role in cell growth and proliferation-related disorders.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed : 31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC) (By similarity). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex (By similarity). In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity).
See full target information EIF2S3

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Journal of ovarian research 15:73 PubMed35718769

2022

Initiation and elongation factor co-expression correlates with recurrence and survival in epithelial ovarian cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Monika Sobočan,Daniela Brunialti,Sussanne Sprung,Christoph Schatz,Jure Knez,Rajko Kavalar,Iztok Takač,Johannes Haybaeck

NPJ genomic medicine 7:17 PubMed35246562

2022

A comprehensive WGS-based pipeline for the identification of new candidate genes in inherited retinal dystrophies.

Applications

Unspecified application

Species

Unspecified reactive species

María González-Del Pozo,Elena Fernández-Suárez,Nereida Bravo-Gil,Cristina Méndez-Vidal,Marta Martín-Sánchez,Enrique Rodríguez-de la Rúa,Manuel Ramos-Jiménez,María José Morillo-Sánchez,Salud Borrego,Guillermo Antiñolo
View all publications

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