protein

Recombinant Human Eukaryotic translation initiation factor 4 gamma 1

MBS956936

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Eukaryotic translation initiation factor 4 gamma 1

Eukaryotic translation initiation factor 4 gamma 1

p220

eukaryotic translation initiation factor 4 gamma 1 isoform 4; Eukaryotic translation initiation factor 4 gamma 1; eukaryotic translation initiation factor 4 gamma 1; p220

EIF4G1

EIF4G1; EIF4G1; P220; EIF4F; EIF4G; EIF4GI; PARK18; EIF-4G1; EIF4F; EIF4G; EIF4GI; eIF-4-gamma 1; eIF-4G 1; eIF-4G1

IF4G1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1250-1599

1404

IEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLE
RSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAE
DMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPL
RPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKE
FLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELN
RQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALM
TAVCYSAIIFETPLRVDVAVL

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Immunology

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.

Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma.Yan R., Rychlik W., Etchison D., Rhoads R.E.J. Biol. Chem. 267:23226-23231(1992) A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A) -binding protein and functions in poly(A) -dependent translation.Imataka H., Gradi A., Sonenberg N.EMBO J. 17:7480-7489(1998) A novel functional human eukaryotic translation initiation factor 4G.Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N.Mol. Cell. Biol. 18:334-342(1998) Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons.Byrd M.P., Zamora M., Lloyd R.E.Mol. Cell. Biol. 22:4499-4511(2002) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) The DNA sequence, annotation and analysis of human chromosome 3.Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.Nature 440:1194-1198(2006)

302699239

NP_004944.3

NM_004953.4

Q04637

67kD

AUF1 (hnRNP D0) Binds And Destabilizes MRNA Pathway (1269726); Activation Of The MRNA Upon Binding Of The Cap-binding Complex And EIFs, And Subsequent Binding To 43S Pathway (1268683); Antiviral Mechanism By IFN-stimulated Genes Pathway (1269316); Cap-dependent Translation Initiation Pathway (1268680); Cytokine Signaling In Immune System Pathway (1269310); Deadenylation Of MRNA Pathway (1269713); Deadenylation-dependent MRNA Decay Pathway (1269712); Eukaryotic Translation Initiation Pathway (1268679); GTP Hydrolysis And Joining Of The 60S Ribosomal Subunit Pathway (1268686); Gene Expression Pathway (1269649)

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq, Aug 2010]

eIF4G: 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. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with CIRBP and MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis. Interacts with RBM4. Belongs to the eIF4G family. 5 isoforms of the human protein are produced by alternative splicing. Protein type: Translation initiation; RNA-binding; Translation. Chromosomal Location of Human Ortholog: 3q27.1. Cellular Component: cytoplasm; cytosol; eukaryotic translation initiation factor 4F complex; membrane. Molecular Function: eukaryotic initiation factor 4E binding; protein binding; translation factor activity, nucleic acid binding; translation initiation factor activity. Biological Process: behavioral fear response; cellular protein metabolic process; cytokine and chemokine mediated signaling pathway; gene expression; insulin receptor signaling pathway; mRNA catabolic process, deadenylation-dependent decay; mRNA catabolic process, nonsense-mediated decay; poly(A) tail shortening; positive regulation of neuron differentiation; regulation of mRNA stability; regulation of translational initiation; translation; translational initiation; viral reproduction

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750