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|Position:||Membrane Protein||Type:||7-transmembrane Protein|
|Appearance:||Lyophilized Or Liquid||MW:||39kDa|
|Expression Material:||E. Coli Extract||Tool:||Nanodisc|
Nanodiscs Tools Cell Free Protein,
Rhodopsin Cell Free Protein,
Proteorhodopsin Cell Free Protein
We supply Proteo rhodopsin, pRhodopsin, Proteorhodopsin rhodopsin, made by cell-free system by nanodiscs tools.
Our cell-free protein has been Function verificated.
Proteorhodopsin (also known as pRhodopsin) is a family of over 50 photoactive retinylidene proteins, a larger family of transmembrane proteins that use retinal as a chromophore for light-mediated functionality, in this case, a proton pump. Some homologues exist as pentamers or hexamers. pRhodopsin is found in marine planktonic bacteria, archaea and eukaryotes (protae), but was first discovered in bacteria.
Proteorhodopsin belongs to a family of similar retinylidene proteins, most similar to its archeal homologes halorhodopsin and bacteriorhodopsin. Bacteriorhodopsin and Halorhodopsin both only exist in the Archea domain whereas proteorhodopsin spans bacteria, archea, and eukaryotes. Proteorhodopsin shares seven transmembrane α-helices retinal covalently linked by a Schiff base mechanism to a lysine residue in the seventh helix (helix G). Bacteriorhodopsin, like proteorhodopsin, is a light-driven proton pump. Sensory Rhodopsin is a G-coupled protein involved in sight.
Proteorhodopsin functions throughout the Earth's oceans as a light-driven H+ pump, by a mechanism similar to that of bacteriorhodopsin. As in bacteriorhodopsin, the retinal chromophoreof proteorhodopsin is covalently bound to the apoprotein via a protonated Schiff base at Lys231. The configuration of the retinal chromophore in unphotolyzed proteorhodopsin is predominantly all-trans, and isome rizes to 13-cis upon illumination with light. Several models of the complete proteorhodopsin photocycle have been proposed, based on FTIR and UV–visible spectroscopy; they resemble established photocycle models for bacteriorhodopsin. Complete proteorhodopsin based photosystems have been discovered and expressed in E. coli, giving them additional light mediated energy gradient capability for ATP generation without external need for retinal or precursors; with the PR, gene five other proteins code for the photopigment biosynthetic pathyway.
Advantage of E.Coli system