EIF4A2 Protein, Human (GST)

EIF4A2, an ATP-dependent RNA helicase, is a vital subunit of the eIF4F complex, pivotal in cap recognition and mRNA binding to ribosomes. In translation initiation, EIF4A2 crucially unwinds RNA secondary structures in mRNA 5'-UTRs. This activity facilitates small ribosomal subunit binding and efficient scanning for the initiator codon, orchestrating translation initiation. EIF4A2 Protein, Human (GST) is the recombinant human-derived EIF4A2 protein, expressed by E. coli, with N-GST labeled tag. The total length of EIF4A2 Protein, Human (GST) is 407 a.a., with molecular weight of 73.4 kDa.

EIF4A2, an ATP-dependent RNA helicase, operates as a crucial subunit within the eIF4F complex, playing a pivotal role in cap recognition and facilitating the binding of mRNA to ribosomes. In the established model of translation initiation, EIF4A2 takes on the responsibility of unwinding RNA secondary structures present in the 5'-UTR of mRNAs. This unwinding activity is essential to create a conducive environment for the efficient binding of the small ribosomal subunit and subsequent scanning for the initiator codon, thus orchestrating the intricate process of translation initiation.

Human

E. coli

N-GST

Q14240 (M1-I407)

1974  [NCBI]

MSGGSADYNREHGGPEGMDPDGVIESNWNEIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWKLDTLCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVEEMPMNVADLI

73.4 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.