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Documentos Principais

B0184

Sigma-Aldrich

Bacteriorhodopsin from Halobacterium salinarum

native sequence, lyophilized powder

Sinônimo(s):

BR from H. salinarum, Bacterioopsin, Bacteriorhodopsin from Halobacterium halobium

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About This Item

Número CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.56

fonte biológica

Halobacterium salinarium

Nível de qualidade

Formulário

lyophilized powder

técnica(s)

ligand binding assay: suitable
mass spectrometry (MS): suitable

nº de adesão UniProt

temperatura de armazenamento

2-8°C

Informações sobre genes

Halobacterium salinarium ... OE_RS05715(5953595) , VNG_RS05715(144807)

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Descrição geral

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.
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.

Aplicação

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

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

Ações bioquímicas/fisiológicas

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

Nota de preparo

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.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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Visite a Biblioteca de Documentos

Light-independent phospholipid scramblase activity of bacteriorhodopsin from Halobacterium salinarum
Verchere A, et al.
Scientific reports, 7(1), 9522-9522 (2017)
Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding
Curnow P and Booth PJ
Proceedings of the National Academy of Sciences of the USA, 104(48), 18970-18975 (2007)
Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum
Dummer AM, et al.
Journal of Bacteriology, 193(20), 5658-5667 (2011)
Systematic analysis of protein-detergent complexes applying dynamic light scattering to optimize solutions for crystallization trials
Meyer A, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 71(1), 75-81 (2015)
High production of bacteriorhodopsin from wild type Halobacterium salinarum
Seyedkarimi MS, et al.
Extremophiles : Life Under Extreme Conditions, 19(5), 1021-1028 (2015)

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