Anti-T2A tag (Clone 3H4-3A5) - Biotin (T754-GRP)

2A viral peptide allows robust production of several proteins in a near-stochiometric manner from the same RNA1 by acting as a cis-acting hydrolase element (CHYSEL)2. When ribosomes encounter the 2A viral peptide conserved consensus sequence (Asp-Val/Ile-Glu-X-Asn-Pro-Gly-Pro), a “ribosomal-skip” or “STOP&GO” occurs and a polypeptide is released while translation continues1,2. In this way, multiple proteins can be produced from a single recombinant construct. This system can be used for multicistronic expression in a wide variety of eukaryotic species2. Its efficacy has been demonstrated in many cell types and can be inherited through the mouse germline. 2A peptide was identified in the Aphthoviruses subgroup of the picornavirus family2. In these viruses, a large polyprotein produces multiple proteins from a single open reading frame, with 2A peptide mediating co-translational cleavage between the Gly and Pro at the end of the peptide. The 2A peptide remains fused to the C-terminus of the upstream protein after cleavage. The Pro is added to the N-terminus of the downstream protein. Translation termination release factors eRF1 and eRF3 play a role in release. Of the different 2A peptides available, T2A has the highest cleavage efficiency3. T2A is derived from Thosea asigna virus. 3H4-3A5 is a recombinant peptide antibody developed against a KLH-coupled synthetic peptide corresponding to Thosea asigna virus 2A peptide (CGDVEENPG).