eIF4G1 Antibody

Western Blot: eIF4G1 Antibody [NB100-268] - Whole cell lysate (50 ug) from HeLa and HEK293T cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-eiF4G1/eiF4GI antibody used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes.

Immunoprecipitation: eIF4G1 Antibody [NB100-268] - Whole cell lysate (1.0 mg per IP reaction; 20% of IP loaded) from HeLa cells prepared using NETN lysis buffer. Antibodies: Affinity purified rabbit anti-eiF4G1/eiF4GI antibody used for IP at 6 ug per reaction. eiF4G1/eiF4GI was also immunoprecipitated by rabbit antieiF4G1/eiF4GI antibody. For blotting immunoprecipitated eiF4G1/eiF4GI, rabbit antieiF4G1/eiF4GI antibody was used at 1 ug/ml. Detection: Chemiluminescence with an exposure time of 10 seconds.

• Reactivity: Hu, Po, Mu
• Applications: WB, IP
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Concentration: 1.0 mg/ml

eIF4G1 Antibody Summary

• Immunogen: The immunogen recognized by this antibody maps to a region between residues 575 and 625 of human Eukaryotic Initiation Factor 4 Gamma 1 (NP_886553.2).
• Predicted Species: Mouse (100%). Backed by our 100% Guarantee.
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Gene: EIF4G1
• Purity: Immunogen affinity purified

Applications/Dilutions

• Dilutions:
  • Western Blot 1:1000-1:10000
  • Immunoprecipitation 2-10 ug/mg lysate

Reactivity Notes

Porcine reactivity reported in scientific literature (PMID: 22013195).

Packaging, Storage & Formulations

• Storage: Store at 4C. Do not freeze.
• Buffer: Tris-Citrate/Phosphate (pH 7.0 - 8.0)
• Preservative: 0.09% Sodium Azide
• Concentration: 1.0 mg/ml
• Purity: Immunogen affinity purified

Alternate Names for eIF4G1 Antibody

• DKFZp686A1451
• EIF4F
• eIF-4G 1
• eIF4G1
• EIF-4G1
• eIF-4-gamma 1
• EIF4-gamma
• EIF4GI
• EIF4Gp220
• eucaryotic translation initiation factor 4G
• eukaryotic translation initiation factor 4 gamma 1
• eukaryotic translation initiation factor 4 gamma, 1
• P220

Background

eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for eIF4G1 Antibody (NB100-268)(24)

Publications using NB100-268

• Hernandez-Garcia AD, Columbus DA, Manjarin R et al. Leucine supplementation stimulates protein synthesis and reduces degradation signal activation in muscle of newborn pigs during acute endotoxemia Am. J. Physiol. Endocrinol. Metab. Sep 13 2016 [PMID: 27624100] (WB, Porcine)
• Galicia-Vazquez G, Cencic R, Robert F et al. A cellular response linking eIF4AI activity to eIF4AII transcription. RNA 2012 Jul [PMID: 22589333]
• El-Kadi SW, Suryawan A, Gazzaneo MC et al. Anabolic Signaling and Protein Deposition Are Enhanced by Intermittent as Compared with Continuous Feeding in Skeletal Muscle of Neonates. American Journal of Physiology, Endocrinology and Metabolism. 2012 [PMID: 22215651]
• Gazzaneo MC, Suryawan A, Orellana RA et al. Intermittent bolus feeding has a greater stimulatory effect on protein synthesis in skeletal muscle than continuous feeding in neonatal pigs J Nutr 2011 Dec [PMID: 22013195] (WB, Porcine)
• Cencic R, Hall DR, Robert F et al. Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F. Proc Natl Acad Sci U S A 2011 Jan [PMID: 21191102]
• Sharma A, Hoeffer CA, Takayasu Y et al. Dysregulation of mTOR signaling in fragile X syndrome. J Neurosci 2010 Jan [PMID: 20071534]
• Wilson FA, Suryawan A, Orellana RA et al. Feeding Rapidly Stimulates Protein Synthesis in Skeletal Muscle of Neonatal Pigs by Enhancing Translation Initiation. J Nutr;139(10):1873-1880. 2009 [PMID: 19692527]
• Spurgeon ME, Ornelles DA. The adenovirus E1B 55-kilodalton and E4 open reading frame 6 proteins limit phosphorylation of eIF2alpha during the late phase of infection. J Virol 2009 Oct [PMID: 19605483]
• Suryawan A, Jeyapalan AS, Orellana RA et al. Leucine stimulates protein synthesis in skeletal muscle of neonatal pigs by enhancing mTORC1 activation. Am J Physiol Endocrinol Metab 2008 Oct [PMID: 18682538]
• Wilson FA, Suryawan A, Orellana RA et al. Fed levels of amino acids are required for the somatotropin-induced increase in muscle protein synthesis. Am J Physiol Endocrinol Metab;295(4):E876-883. 2008 [PMID: 18682537]
• Lin CJ, Cencic R, Mills JR et al. c-Myc and eIF4F are components of a feedforward loop that links transcription and translation. Cancer Res 2008 Jul [PMID: 18593934]
• Wilson FA, Orellana RA, Suryawan A et al. Stimulation of muscle protein synthesis by somatotropin in pigs is independent of the somatotropin-induced increase in circulating insulin. Am J Physiol Endocrinol Metab;295(1):E187-194. 2008 [PMID: 18460595]
• Escobar, J et al. Amino acid Availability Age Affect the Leucine Stimulation of Protein Synthesis eIF4F Formation in Muscle. Am J Physiol Endocrinol Metab. 10.1152/ajpendo.00302.2007. 2007 [PMID: 17878223]
• Gelinas JN, Banko JL, Hou L et al. ERK and mTOR signaling couple beta-adrenergic receptors to translation initiation machinery to gate induction of protein synthesis-dependent long-term potentiation. J Biol Chem 2007 Sep [PMID: 17635924]
• Otulakowski G, Duan W, Gandhi S et al. Steroid and oxygen effects on eIF4F complex, mTOR, and ENaC translation in fetal lung epithelia. Am J Respir Cell Mol Biol 2007 Oct [PMID: 17556672]
• Vary TC, Anthony JC, Jefferson LS et al. Rapamycin blunts nutrient stimulation of eIF4G, but not PKCepsilon phosphorylation, in skeletal muscle. Am J Physiol Endocrinol Metab 2007 Jul [PMID: 17389711]
• Bordeleau ME, Cencic R, Lindqvist L et al. RNA-mediated sequestration of the RNA helicase eIF4A by Pateamine A inhibits translation initiation. Chem Biol 2006 Dec [PMID: 17185224]
• Yang R, Weber DJ, Carrier F et al. Post-transcriptional regulation of thioredoxin by the stress inducible heterogenous ribonucleoprotein A18. Nucleic Acids Res 2006 Mar [PMID: 16513844]
• Banko JL, Hou L, Poulin F et al. Regulation of eukaryotic initiation factor 4E by converging signaling pathways during metabotropic glutamate receptor-dependent long-term depression. J Neurosci 2006 Feb [PMID: 16495443]
• Funai K, Parkington JD, Carambula S et al. Age-associated decrease in contraction-induced activation of downstream targets of Akt/mTor signaling in skeletal muscle. Am J Physiol Regul Integr Comp Physiol 2006 Apr [PMID: 16306159]
• Vary TC, Lynch CJ. Meal feeding enhances formation of eIF4F in skeletal muscle: role of increased eIF4E availability and eIF4G phosphorylation. Am J Physiol Endocrinol Metab 2006 Apr [PMID: 16263769]
• Harber MP, Schenk S, Barkan AL et al. Effects of dietary carbohydrate restriction with high protein intake on protein metabolism and the somatotropic axis. J Clin Endocrinol Metab 2005 Sep [PMID: 15972575]
• Vary TC, Deiter G, Goodman SA et al. Acute alcohol intoxication enhances myocardial eIF4G phosphorylation despite reducing mTOR signaling. Am J Physiol Heart Circ Physiol 2005 Jan [PMID: 15388509]
• Lang CH, Frost RA, Svanberg E et al. IGF-I/IGFBP-3 ameliorates alterations in protein synthesis, eIF4E availability, and myostatin in alcohol-fed rats. Am J Physiol Endocrinol Metab 2004 Jun [PMID: 14749210]

Bioinformatics

• Gene Symbol: EIF4G1
• Entrez:
  • 1981(Human)
  • 287986(Rat)
• Uniprot:
  • Q04637()