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EIF4G2 Antibody (monoclonal) (M01)
Mouse monoclonal antibody raised against a partial recombinant EIF4G2.
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC |
|---|---|
| Primary Accession | P78344 |
| Other Accession | NM_001418 |
| Reactivity | Human, Rat |
| Host | mouse |
| Clonality | Monoclonal |
| Isotype | IgG1 Kappa |
| Clone Names | 3B5 |
| Calculated MW | 102362 Da |
| Gene ID | 1982 |
|---|---|
| Other Names | Eukaryotic translation initiation factor 4 gamma 2, eIF-4-gamma 2, eIF-4G 2, eIF4G 2, Death-associated protein 5, DAP-5, p97, EIF4G2 (HGNC:3297) |
| Target/Specificity | EIF4G2 (NP_001409, 811 a.a. ~ 889 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. |
| Dilution | WB~~1:500~1000 |
| Format | Clear, colorless solution in phosphate buffered saline, pH 7.2 . |
| Storage | Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. |
| Precautions | EIF4G2 Antibody (monoclonal) (M01) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three subunits: eIF4A, eIF4E and eIF4G. The protein encoded by this gene shares similarity with the C-terminal region of eIF4G that contains the binding sites for eIF4A and eIF3; eIF4G, in addition, contains a binding site for eIF4E at the N-terminus. Unlike eIF4G, which supports cap-dependent and independent translation, this gene product functions as a general repressor of translation by forming translationally inactive complexes. In vitro and in vivo studies indicate that translation of this mRNA initiates exclusively at a non-AUG (GUG) codon. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.
References
Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5. Frank F, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010 Jan 1. PMID 20057060.Translation of mRNAs from vesicular stomatitis virus and vaccinia virus is differentially blocked in cells with depletion of eIF4GI and/or eIF4GII. Welnowska E, et al. J Mol Biol, 2009 Dec 4. PMID 19769989.Defining the human deubiquitinating enzyme interaction landscape. Sowa ME, et al. Cell, 2009 Jul 23. PMID 19615732.The crystal structure of the C-terminal DAP5/p97 domain sheds light on the molecular basis for its processing by caspase cleavage. Liberman N, et al. J Mol Biol, 2008 Nov 14. PMID 18722383.Death-associated protein 5 (DAP5/p97/NAT1) contributes to retinoic acid-induced granulocytic differentiation and arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Ozpolat B, et al. Apoptosis, 2008 Jul. PMID 18491231.
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