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Bacteriorhodopsin from Halobacterium salinarum

SIGMA/B0184 - native sequence, lyophilized powder

Synonym: BR from H. salinarum; Bacterioopsin; Bacteriorhodopsin from Halobacterium halobium

CAS Number: 53026-44-1
MDL Number: MFCD00130599
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-B0184-1MG 1 mg
$1090.00
1/EA
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45-B0184-5MG 5 mg
$4200.00
1/EA
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biological source Halobacterium salinarium
form lyophilized powder
Quality Level 100 
storage temp. 2-8°C
technique(s) ligand binding assay: suitable
  mass spectrometry (MS): suitable
UniProt accession no. B0R5N9 
Application: Bacteriorhodopsin from Halobacterium salinarum has been used:
• in generation of droplet lipid bilayer
• as a standard in quadrupole time-of-flight (QTOF) mass spectroscopy (MS)
• in the generation of protein-detergent complex and micelles for dynamic light scattering studies

Application: Bacteriorhodopsin is of interest in the development of artificial retinas, optical associative processors, and three-dimensional memory storage devices.
Biochem/physiol Actions: A transmembrane retinylidine protein that functions as a proton pump driven by light energy in Holobacterium.
Biochem/physiol Actions: Bacteriorhodopsin (BR) from Halobacterium salinarum acts as a proton-driven pump. BR can be used in studies of the folding and kinetics of α-helical proteins. It is thermally stable and exhibits high photoelectric and photochemical efficiency. BR exists as trimer in a hexagonal lattice. Its photocycle intermediates are exploited in bioelectronics majorly in photoelectric and photochemical applications.
General description: Bacteriorhodopsin (BR) is a covalent complex comprising bacterioopsin protein and retinal cofactor in the equimolar ratio. It corresponds to the molecular weight of 27kDa. BR belongs to the retinylidene class of proteins. It 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 β-helical proteins.
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.
Preparation Note: Wild-type bacteriorhodopsin is isolated from Halobacterium salinarum strain S9 as purple membranes.
RIDADR NONH for all modes of transport
WGK Germany WGK 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
Storage Temp. 2-8°C
UNSPSC 12352202

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