EIF2A Antibody
Purified Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC, FC, ICC, E |
---|---|
Primary Accession | Q9BY44 |
Reactivity | Human |
Host | Mouse |
Clonality | Monoclonal |
Clone Names | 3A7A8 |
Isotype | IgG1 |
Calculated MW | 65kDa |
Description | EIF2A is a 65-kD protein that catalyzes the formation of puromycin-sensitive 80S preinitiation complexes |
Immunogen | Purified recombinant fragment of human EIF2A (AA: 448-576) expressed in E. Coli. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
Gene ID | 83939 |
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Other Names | Eukaryotic translation initiation factor 2A, eIF-2A, 65 kDa eukaryotic translation initiation factor 2A, Eukaryotic translation initiation factor 2A, N-terminally processed, EIF2A |
Dilution | E~~1/10000 WB~~1/500 - 1/2000 IF~~1/200 - 1/1000 FC~~1/200 - 1/400 IHC~~1/200 - 1/1000 |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | EIF2A Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | EIF2A |
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Function | Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl- tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. |
Tissue Location | Widely expressed. Expressed at higher level in pancreas, heart, brain and placenta. |

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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic. ; ; ;
References
1. Mol Biol (Mosk). 2010 Sep-Oct;44(5):859-66. 2. Cancer Res. 2009 Feb 15;69(4):1545-52.

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