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B0184 Sigma

Bacteriorhodopsin from Halobacterium salinarum

native sequence, lyophilized powder




Bacteriorhodopsin is of interest in the development of artificial retinas, optical associative processors, and three-dimensional memory storage devices.

Bacteriorhodopsin (BR) from Halobacterium salinarum is a seven-membrane helical protein that acts as a photon-driven pump. BR can be used in studies of the folding and kenetics of á-helical proteins.

Biochem/physiol Actions

A transmembrane retinylidine protein that functions as a proton pump driven by light energy in Holobacterium.

General description

Bacteriorhodopsin is the prototypical "seven-helix" transmembrane protein (with seven α-helical domains), whose study led to advances in understanding G protein-coupled receptors (GPCRs). In Halobacteria, it acts as a light-harvesting protein, producing a proton gradient across the cell wall that is then used to drive biosynthetic processes.

Preparation Note

Aqueous suspensions may be sonicated to achieve the desired homogeneity and may be stored for a short time at a temperature of 2-8 °C or at a temperature of -20 °C without time limitation.

Wild-type bacteriorhodopsin is isolated from Halobacterium salinarum strain S9 as purple membranes.

Price and Availability

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Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

Protocols & Articles


Fluorescent G protein-coupled receptors (GPCRs)

G protein-coupled receptors (GPCRs) are the largest class of transmembrane proteins and the targets for almost half of the clinical drugs in the market today. Advances in X-ray crystallography and ot...
Mike Earley, Market Segment Manager, Sigma Life Science
Biofiles Vol. 8, No. 4
Keywords: Clinical, Confocal microscopy, Ligands, Microscopy

Peer-Reviewed Papers


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