Eukaryotic Translation Initiation Factor 5 (EIF5) (AA 100-215) antibody

Antigen: Eukaryotic Translation Initiation Factor 5 (EIF5)

Synonyms: EIF-5A, MGC36374, MGC36509, D12Ertd549e, 2810011H21Rik, fb37c12, fb54h04, zgc:56606, zgc:77026, wu:fb37c12, wu:fb54h04

Binding Site: AA 100-215

Clonality: Monoclonal (20)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF)

Catalog no.: ABIN968343

Additional Information

Alternative name: eIF-5

Immunogen: Human eIF-5

Cross-Reactivity: Mouse (Murine), Rat (Rattus)

Format: Liquid

Isotype: IgG1

Clone: 20

Description: Initiation of eukaryotic translation involves a series of reactions mediated by multiple eukaryotic initiation factors (eIFs). As a prerequisite to initiation, the initiator methionyl-tRNA (Met-tRNAf), in a ternary complex with eIF-2 and GTP, binds to the 40S ribosomal subunit. This 40S preinitiation complex is positioned at the initiation AUG codon to form the 40S initiation complex. This complex is joined by the 60S ribosomal subunit to form the 80S initiation complex, which functions as a peptidyl transferase. The joining of the 60S subunit to the 40S initiation complex requires eIF-5. This protein associates with the 40S initiation complex, specifically with the beta subunit of eIF-2, prior to binding of the 60S subunit. eIF-5 induces GTP hydrolysis of the ternary complex bound to the 40S ribosome. This results in the release of eIF-2 and GDP from the 40S subunit and allows for interaction with the 60S subunit. Furthermore, eIF-5 is thought to be involved in recognition of the start codon and interacts with eIF-3, an additional factor required for 40S initiation complex formation. Thus, eIF-5 is essential to the assembly and proper function of the eukaryotic machinery. eIF-5 has a calculated molecular weight of 49 kDa, but has been reported to migrate in a range between 49-53 kDa.
Synonyms: Eukaryotic Initiation Factor-5

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Molecular Weight: 49-53 kDa

Comments:

Related Products: ABIN968587, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20°C.

Restrictions: For Research Use only

Images

Western blot analysis of eIF-5 on a HepG2 cell lysate (Human hepatocellular carcinoma, ATCC HB-8065). Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the mouse anti- eIF-5 antibody.

Immunofluorescence staining of WI-38 cells (Human lung fibroblasts, ATCC CCL-75).

anti-Eukaryotic Translation Initiation Factor 5 (EIF5) (AA 100-215) antibody (Image 3)

Publications

Product: Chevesich, Chaudhuri, Maitra: "Characterization of mammalian translation initiation factor 5 (eIF-5). Demonstration that eIF-5 is a phosphoprotein and is present in cells as a single molecular form of apparent M(r) 58,000." in: The Journal of biological chemistry, Vol. 268, Issue 27, pp. 20659-67, 1993 (PubMed).

Si, Das, Maitra: "Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5)." in: The Journal of biological chemistry, Vol. 271, Issue 28, pp. 16934-8, 1996 (PubMed).

Das, Maiti, Das et al.: "Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the beta-subunit of eIF2." in: The Journal of biological chemistry, Vol. 272, Issue 50, pp. 31712-8, 1998 (PubMed).

Phan, Zhang, Asano et al.: "Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5." in: Molecular and cellular biology, Vol. 18, Issue 8, pp. 4935-46, 1998 (PubMed).

Kedersha, Chen, Gilks et al.: "Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules." in: Molecular biology of the cell, Vol. 13, Issue 1, pp. 195-210, 2002 (PubMed).