When I use the N-terminal fusion vectors (pTYB11 and pTYB12), how do I remove the small peptide co-eluted with the target protein?
Dialysis will remove the small peptide (1.2 kDa) that is co-eluted with the target protein. Due to its small molecular weight, the N-extein cleaved peptide can not be detected on a regular SDS-PAGE gel free DTT from solution, and the DTT moiety will be released from the carboxyl terminus of the target protein following cleavage (See Appendix III in IMPACT-CN manual).
Related Questions
- In the case of the N-terminal fusion vectors (pTYB11 and 12), which residues at the N-terminal of the target protein may inhibit cleavage or cause in vivo cleavage?
- When I use the N-terminal fusion vectors (pTYB21, pTYB22, pTYB11 and pTYB12), how do I remove the small peptide co-eluted with the target protein?
- When I use the N-terminal fusion vectors (pTYB11 and pTYB12), how do I remove the small peptide co-eluted with the target protein?
