EIF4A1 Protein, Human (His, Strep)

The EIF4A1 protein is an ATP-dependent RNA helicase and an important subunit of the eIF4F complex, which is essential for cap recognition and promoting the binding of mRNA to ribosomes. In the translation initiation model, EIF4A1 helps unravel RNA secondary structure in the mRNA 5'-UTR. EIF4A1 Protein, Human (His, Strep) is the recombinant human-derived EIF4A1 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of EIF4A1 Protein, Human (His, Strep) is 406 a.a., .

EIF4A2, an ATP-dependent RNA helicase, functions as a crucial subunit of the eIF4F complex, playing a key role in cap recognition and facilitating mRNA binding to the ribosome. In the prevailing model of translation initiation, EIF4A2 is instrumental in unwinding RNA secondary structures present in the 5'-UTR of mRNAs. This unwinding activity is essential to enable the efficient binding of the small ribosomal subunit and subsequent scanning for the initiator codon, a fundamental process in the initiation of translation.

Human

E. coli

N-Strep;N-6*His

P60842 (M1-I406)

1973

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

<1 EU/μg, determined by LAL method.