Human eIF4G Recombinant Protein

Reference:
Size

100ug, 50ug

Brand

Product type

Host Species

Applications

,

Product nameHuman eIF4G Recombinant Protein
Origin speciesHomo sapiens (Human)
Expression systemProkaryotic expression
SequenceMGSHHHHHHSGMSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLAESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANK
Molecular weight23.49kDa
Protein delivered with Tag?N-ter His&Trx Tag
Purity estimated≥95%
BufferPBS, imidazole 200mM + 50% glycérol
Formliquid
Delivery conditionDry Ice
Delivery lead time in business days2-3
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
Fragment TypeGlu557~Lys646
Protein AccessionEAW78268.1
NCBI ReferenceWP_001583586
Aliases /SynonymsEIF-4G1, EIF4F, EIF4G, EIF4GI, P220, PARK18
ReferencePX-P2069
NoteFor research use only

Description of Human eIF4G Recombinant Protein

The Structure of Human eIF4G Recombinant Protein

Human eIF4G (eukaryotic initiation factor 4G) is a large multidomain protein that plays a crucial role in the initiation of protein synthesis in eukaryotic cells. It is a key component of the eIF4F complex, which is responsible for recruiting the 40S ribosomal subunit to the 5′ end of mRNA, allowing for the initiation of translation. The eIF4G protein is composed of three major domains: the N-terminal domain, the central domain, and the C-terminal domain.

The N-terminal domain of eIF4G is responsible for binding to eIF4E, the cap-binding protein, and forming the eIF4F complex. This domain also contains binding sites for other eIF4 proteins, such as eIF4A and eIF4B, which are involved in unwinding the mRNA secondary structure. The central domain of eIF4G contains multiple HEAT repeats, which are structural motifs that facilitate protein-protein interactions. This domain is responsible for binding to eIF3, another key component of the translation initiation complex. The C-terminal domain of eIF4G contains a binding site for the poly(A)-binding protein (PABP), which is responsible for recruiting the 60S ribosomal subunit to the mRNA.

The Activity of this protein

As mentioned earlier, eIF4G plays a crucial role in the initiation of protein synthesis. It is involved in multiple steps of this process, including binding to the mRNA cap, recruiting the ribosome, and promoting mRNA unwinding. The eIF4G protein also interacts with other translation initiation factors, such as eIF3 and PABP, to facilitate the formation of the translation initiation complex.

One of the key activities of eIF4G is its ability to bind to eIF4E and form the eIF4F complex. This interaction is essential for the recruitment of the 40S ribosomal subunit to the mRNA, as eIF4E is responsible for recognizing and binding to the mRNA cap structure. Additionally, the central domain of eIF4G plays a crucial role in promoting the unwinding of mRNA secondary structures, allowing for efficient translation initiation.

Another important activity of eIF4G is its interaction with eIF3. This interaction is crucial for the assembly of the 43S pre-initiation complex, which consists of the 40S ribosomal subunit, eIF3, and other initiation factors. The eIF4G-eIF3 interaction also helps to position the mRNA in the correct orientation for translation initiation.

The Application of Human eIF4G Recombinant Protein

Given its crucial role in protein synthesis, eIF4G has been identified as a potential drug target for various diseases. Dysregulation of translation initiation has been linked to several diseases, including cancer, viral infections, and neurological disorders. In cancer, for example, overexpression of eIF4G has been observed in many types of tumors, and targeting eIF4G has been shown to inhibit tumor growth. This makes eIF4G an attractive target for the development of anticancer therapies.

In addition to its potential as a drug target, eIF4G recombinant protein has also been used in various research applications. It can be used to study the mechanisms of translation initiation and its role in various diseases. Recombinant eIF4G can also be used in in vitro translation assays to investigate the effects of different factors on translation efficiency.

In conclusion, Human eIF4G recombinant protein is a crucial component of the translation initiation complex, with a well-defined structure and multiple activities that are essential for efficient protein synthesis. Its potential as a drug target and its applications in research make it a valuable protein for further study.

Publication

  • 1: Nichols N, Bras JM, Hernandez DG, Jansen IE, Lesage S, Lubbe S, Singleton AB; International Parkinson's Disease Genomics Consortium.. EIF4G1 mutations do not cause Parkinson's disease. Neurobiol Aging. 2015 Aug;36(8):2444.e1-4. doi: 10.1016/j.neurobiolaging.2015.04.017. Epub 2015 May 9. PubMed PMID: 26022768; PubMed Central PMCID: PMC4464946.
  • 2: Deng H, Wu Y, Jankovic J. The EIF4G1 gene and Parkinson's disease. Acta Neurol Scand. 2015 Aug;132(2):73-8. doi: 10.1111/ane.12397. Epub 2015 Mar 13. Review. PubMed PMID: 25765080.
  • 3: Huttenlocher J, Krüger R, Capetian P, Lohmann K, Brockmann K, Csoti I, Klein C, Berg D, Gasser T, Bonin M, Riess O, Bauer P. EIF4G1 is neither a strong nor a common risk factor for Parkinson's disease: evidence from large European cohorts. J Med Genet. 2015 Jan;52(1):37-41. doi: 10.1136/jmedgenet-2014-102570. Epub 2014 Nov 3. PubMed PMID: 25368108.
  • 4: Akabayov SR, Akabayov B, Wagner G. Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex. Biochemistry. 2014 Oct 21;53(41):6422-5. doi: 10.1021/bi500600m. Epub 2014 Oct 8. PubMed PMID: 25255371; PubMed Central PMCID: PMC4204880.
  • 5: Attar-Schneider O, Drucker L, Zismanov V, Tartakover-Matalon S, Lishner M. Targeting eIF4GI translation initiation factor affords an attractive therapeutic strategy in multiple myeloma. Cell Signal. 2014 Sep;26(9):1878-87. doi: 10.1016/j.cellsig.2014.05.005. Epub 2014 May 9. PubMed PMID: 24815186.
  • 6: Nishioka K, Funayama M, Vilariño-Güell C, Ogaki K, Li Y, Sasaki R, Kokubo Y, Kuzuhara S, Kachergus JM, Cobb SA, Takahashi H, Mizuno Y, Farrer MJ, Ross OA, Hattori N. EIF4G1 gene mutations are not a common cause of Parkinson's disease in the Japanese population. Parkinsonism Relat Disord. 2014 Jun;20(6):659-61. doi: 10.1016/j.parkreldis.2014.03.004. Epub 2014 Mar 18. PubMed PMID: 24704100; PubMed Central PMCID: PMC4034257.
  • 7: Blanckenberg J, Ntsapi C, Carr JA, Bardien S. EIF4G1 R1205H and VPS35 D620N mutations are rare in Parkinson's disease from South Africa. Neurobiol Aging. 2014 Feb;35(2):445.e1-3. doi: 10.1016/j.neurobiolaging.2013.08.023. Epub 2013 Sep 27. PubMed PMID: 24080171.
  • 8: Li K, Tang BS, Guo JF, Lou MX, Lv ZY, Liu ZH, Tian Y, Song CY, Xia K, Yan XX. Analysis of EIF4G1 in ethnic Chinese. BMC Neurol. 2013 Apr 26;13:38. doi: 10.1186/1471-2377-13-38. PubMed PMID: 23617574; PubMed Central PMCID: PMC3663786.
  • 9: Yuan L, Song Z, Xu H, Gu S, Zhu A, Gong L, Zhao Y, Deng H. EIF4G1 Ala502Val and Arg1205His variants in Chinese patients with Parkinson disease. Neurosci Lett. 2013 May 24;543:69-71. doi: 10.1016/j.neulet.2013.02.056. Epub 2013 Apr 2. PubMed PMID: 23562511.
  • 10: Siitonen A, Majounie E, Federoff M, Ding J, Majamaa K, Singleton AB. Mutations in EIF4G1 are not a common cause of Parkinson's disease. Eur J Neurol. 2013 Apr;20(4):e59. doi: 10.1111/ene.12051. PubMed PMID: 23490116.
  • 11: Dobrikov MI, Dobrikova EY, Gromeier M. Dynamic regulation of the translation initiation helicase complex by mitogenic signal transduction to eukaryotic translation initiation factor 4G. Mol Cell Biol. 2013 Mar;33(5):937-46. doi: 10.1128/MCB.01441-12. Epub 2012 Dec 21. PubMed PMID: 23263986; PubMed Central PMCID: PMC3623071.
  • 12: Fujioka S, Sundal C, Strongosky AJ, Castanedes MC, Rademakers R, Ross OA, Vilariño-Güell C, Farrer MJ, Wszolek ZK, Dickson DW. Sequence variants in eukaryotic translation initiation factor 4-gamma (eIF4G1) are associated with Lewy body dementia. Acta Neuropathol. 2013 Mar;125(3):425-38. doi: 10.1007/s00401-012-1059-4. Epub 2012 Nov 4. PubMed PMID: 23124435; PubMed Central PMCID: PMC3580022.
  • 13: Badura M, Braunstein S, Zavadil J, Schneider RJ. DNA damage and eIF4G1 in breast cancer cells reprogram translation for survival and DNA repair mRNAs. Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18767-72. doi: 10.1073/pnas.1203853109. Epub 2012 Oct 29. PubMed PMID: 23112151; PubMed Central PMCID: PMC3503184.
  • 14: Zhao Y, Ho P, Prakash KM, Foo JN, Liu JJ, Au WL, Tan LC, Tan EK. Analysis of EIF4G1 in Parkinson's disease among Asians. Neurobiol Aging. 2013 Apr;34(4):1311.e5-6. doi: 10.1016/j.neurobiolaging.2012.09.003. Epub 2012 Oct 23. PubMed PMID: 23092605.
  • 15: Kumar KR, Lohmann K, Klein C. Genetics of Parkinson disease and other movement disorders. Curr Opin Neurol. 2012 Aug;25(4):466-74. doi: 10.1097/WCO.0b013e3283547627. Review. PubMed PMID: 22772876.
  • 16: Schulte EC, Mollenhauer B, Zimprich A, Bereznai B, Lichtner P, Haubenberger D, Pirker W, Brücke T, Molnar MJ, Peters A, Gieger C, Trenkwalder C, Winkelmann J. Variants in eukaryotic translation initiation factor 4G1 in sporadic Parkinson's disease. Neurogenetics. 2012 Aug;13(3):281-5. doi: 10.1007/s10048-012-0334-9. Epub 2012 Jun 16. PubMed PMID: 22707335.
  • 17: Lesage S, Condroyer C, Klebe S, Lohmann E, Durif F, Damier P, Tison F, Anheim M, Honoré A, Viallet F, Bonnet AM, Ouvrard-Hernandez AM, Vidailhet M, Durr A, Brice A; French Parkinson's Disease Genetics Study Group.. EIF4G1 in familial Parkinson's disease: pathogenic mutations or rare benign variants? Neurobiol Aging. 2012 Sep;33(9):2233.e1-2233.e5. doi: 10.1016/j.neurobiolaging.2012.05.006. Epub 2012 Jun 1. PubMed PMID: 22658323.

Reviews

There are no reviews yet.

REVIEW YOUR PRODUCT

Be the first to review “Human eIF4G Recombinant Protein”

Your email address will not be published. Required fields are marked *

Contact us

Send us a message from the form below







    Cart (0 Items)

    Your cart is currently empty.

    View Products