eGFP, for example, can be fused to the C- terminal of your target protein. Fluorescent proteins were usually highly soluble, especially if you select to express in insect cells, which has the tendency to express proteins in soluble states.
Smith | | Smith Liu | | 邮箱：[email protected] | 签名由 网易邮箱大师 定制 On 12/07/2021 07:21, samer halabi wrote: Dear All, Sorry for disturbing you all with my current inquiry. However, I am in the process of designing and expressing soluble proteins and I thought to ask for your valuable advice. 1-What would be your first choice (protein-based) fluorophore to link it to the soluble protein at its C-terminus? 2-Would this fluorophore be suitable for carrying later experiments in vivo and in vitro withstanding such conditions and still having detectable fluorescence signal (medium to high)? 3-Would this fluorophore of choice stand denaturing and renaturing conditions, as refolding the protein chimera (soluble protein + the linked fluorophore) from bacterial inclusion bodies that were dissolved in 8M Urea or 6M Guanidine-HCl? 4-Have you had success with producing APC or R-PE in such manner (secreting them from insect cells or refolding them from bacterial inclusion bodies)? Thank you in advance. Best regards, Samer To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
