|Application ||WB, IHC-P, E|
|Dilution||IHC-P (5 µg/ml)|
|Other Names||Eukaryotic translation initiation factor 2 subunit 3, Eukaryotic translation initiation factor 2 subunit gamma X, eIF-2-gamma X, eIF-2gX, EIF2S3, EIF2G|
|Target/Specificity||Human EIF2S3 / EIF2G|
|Reconstitution & Storage||Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles.|
|Precautions||EIF2S3 / EIF2G Antibody (clone 1H3) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (By similarity).|
|Tissue Location||Expressed in testis, brain, liver and muscle.|
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Provided below are standard protocols that you may find useful for product applications.
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
Gaspar N.J.,et al.J. Biol. Chem. 269:3415-3422(1994).
Goshima N.,et al.Nat. Methods 5:1011-1017(2008).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Gevaert K.,et al.Nat. Biotechnol. 21:566-569(2003).
Bienvenut W.V.,et al.Submitted (DEC-2008) to UniProtKB.
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