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EIF4G1 recombinant protein :: Eukaryotic translation initiation factor 4 gamma 1 Recombinant Protein

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Catalog # MBS956936
Unit / Price
  0.01 mg (Yeast)  /  $110 +1 FREE 8GB USB
  0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $190 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
  0.1 mg (Yeast)  /  $285 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $460 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $750 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $1,010 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,180 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,255 +1 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,280 +1 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $1,845 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $1,905 +2 FREE 8GB USB
  1 mg (Baculovirus)  /  $2,450 +3 FREE 8GB USB
SDS-Page
Product Name

Eukaryotic translation initiation factor 4 gamma 1 (EIF4G1), Recombinant Protein

Popular Item
Also Known As

Recombinant Human Eukaryotic translation initiation factor 4 gamma 1

Product Synonym Names
p220
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1250-1599aa; Partial
Sequence Length
1404
Sequence
IEEYLHLNDM KEAVQCVQEL ASPSLLFIFV RHGVESTLER SAIAREHMGQ LLHQLLCAGH LSTAQYYQGL YEILELAEDM EIDIPHVWLY LAELVTPILQ EGGVPMGELF REITKPLRPL GKAASLLLEI LGLLCKSMGP KKVGTLWREA GLSWKEFLPE GQDIGAFVAE QKVEYTLGEE SEAPGQRALP SEELNRQLEK LLKEGSSNQR VFDWIEANLS EQQIVSNTLV RALMTAVCYS AIIFETPLRV DVAVLKARAK LLQKYLCDEQ KELQALYALQ ALVVTLEQPP NLLRMFFDAL YDEDVVKEDA FYSWESSKDP AEQQGKGVAL KSVTAFFKWL REAEEESDHN
OMIM
600495
3D Structure
ModBase 3D Structure for Q04637
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of EIF4G1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
EIF4G1 recombinant protein
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.
Product Categories/Family for EIF4G1 recombinant protein

EIF4G1 recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for EIF4G1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
Molecular Weight
67kD
NCBI Official Full Name
eukaryotic translation initiation factor 4 gamma 1 isoform 4
NCBI Official Synonym Full Names
eukaryotic translation initiation factor 4 gamma 1
NCBI Official Symbol
EIF4G1  [Similar Products]
NCBI Official Synonym Symbols
P220; EIF4F; EIF4G; EIF4GI; PARK18; EIF-4G1
  [Similar Products]
UniProt Protein Name
Eukaryotic translation initiation factor 4 gamma 1
UniProt Synonym Protein Names
p220
UniProt Gene Name
EIF4G1  [Similar Products]
UniProt Synonym Gene Names
EIF4F; EIF4G; EIF4GI; eIF-4-gamma 1; eIF-4G 1; eIF-4G1  [Similar Products]
UniProt Entry Name
IF4G1_HUMAN
NCBI Summary for EIF4G1
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]
UniProt Comments for EIF4G1
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
Product References and Citations for EIF4G1 recombinant protein
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)

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