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07-1800

Sigma-Aldrich

Anti-eIF4G Antibody

serum, from rabbit

Sinónimos:

eIF-4-gamma 1, eIF-4G 1, eukaryotic translation initiation factor 4 gamma 1

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, mouse

technique(s)

immunofluorescence: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... EIF4G1(1981)

General description

eIF4F is a translation initiation factor containing three subunits: eIF4A, eIF4E, and eIF4G. This complex is a key component in promoting ribosomal binding to the mRNA. eIF4G interacts with both eIF4A and eIF4E though its carboxy and amino terminal domains, respectively. eIF4E binds to the cap structure of the mRNA, while the ATP-dependent RNA helicase eIF4A unwinds the secondary structure of the 5’ UTR. eIF4G plays a critical role in coordinating the assembly of the eukaryotic initiation factors. It acts as a bridge to bind the cap-bound eIF4E, eIF4AI&II, the eIF3 complex, PABP1, and the kinase Mnk1 (Lejeune, F., et al., 2004) in a large eukaryotic initiation factor complex

Specificity

Not tested on other species.
This antibody detects eIF4G at its N-terminal region.

Immunogen

Epitope: N-terminus
Synthetic peptide corresponding to N-terminal region of human eIF4G.

Application

Anti-eIF4G Antibody is an antibody against eIF4G for use in WB & IF.
Research Category
Signaling
Research Sub Category
RNA Binding Protein (RBP)

Insulin/Energy Signaling

Quality

Evaluated by western blot on HeLa cytoplasmic extract.

Western Blot Analysis: 1:1,000 dilution of this antibody was used to detect eIF4G in HeLa cytoplasmic extract and lysates from 293T and S10 cells.

Target description

220 kDa

Physical form

Rabbit polyclonal serum with 0.05% NaN3.

Storage and Stability

Stable for 1 year at -20ºC from date of receipt.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids


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Daniel A Columbus et al.
American journal of physiology. Endocrinology and metabolism, 309(6), E601-E610 (2015-09-17)
Most low-birth weight infants experience extrauterine growth failure due to reduced nutrient intake as a result of feeding intolerance. The objective of this study was to determine whether prolonged enteral leucine supplementation improves lean growth in neonatal pigs fed a
Huanru Wang et al.
International journal of molecular sciences, 20(19) (2019-10-03)
Signal transducer and activator of transcription 3 (STAT3) is a multifunctional factor that regulates inflammation and immunity. Knowledge of its regulatory mechanisms is very limited. Here, we showed that enterovirus 71 (EV71) infection induced the phosphorylation of STAT3 and the
Marko Rudar et al.
American journal of physiology. Endocrinology and metabolism, 320(3), E551-E565 (2021-01-12)
Extrauterine growth restriction in premature infants is largely attributed to reduced lean mass accretion and is associated with long-term morbidities. Previously, we demonstrated that prematurity blunts the feeding-induced stimulation of translation initiation signaling and protein synthesis in skeletal muscle of
Marko Rudar et al.
American journal of physiology. Endocrinology and metabolism, 321(6), E737-E752 (2021-11-02)
Optimizing enteral nutrition for premature infants may help mitigate extrauterine growth restriction and adverse chronic health outcomes. Previously, we showed in neonatal pigs born at term that lean growth is enhanced by intermittent bolus compared with continuous feeding. The objective
Anat Bahat et al.
EMBO molecular medicine, 16(3), 523-546 (2024-02-20)
Huntington's disease (HD) is an incurable inherited disorder caused by a repeated expansion of glutamines in the huntingtin gene (Htt). The mutant protein causes neuronal degeneration leading to severe motor and psychological symptoms. Selective downregulation of the mutant Htt gene

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