Saltar al contenido
Merck
Todas las fotos(1)

Key Documents

B0184

Sigma-Aldrich

Bacteriorhodopsin from Halobacterium salinarum

native sequence, lyophilized powder

Sinónimos:

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

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.56

biological source

Halobacterium salinarium

form

lyophilized powder

technique(s)

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

UniProt accession no.

storage temp.

2-8°C

Gene Information

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

¿Está buscando productos similares? Visita Guía de comparación de productos

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.
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.

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

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

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

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

A review on bacteriorhodopsin-based bioelectronic devices
Li YT, et al.
Sensors, 18(5), 1368-1368 (2018)
Jonathan P Schlebach et al.
Protein science : a publication of the Protein Society, 21(1), 97-106 (2011-11-19)
The elucidation of the physical principles that govern the folding and stability of membrane proteins is one of the greatest challenges in protein science. Several insights into the folding of α-helical membrane proteins have come from the investigation of the
Light-Patterned Current Generation in a Droplet Bilayer Array
Schild V, et al.
Scientific reports, 7, 46585-46585 (2017)
Best practices and benchmarks for intact protein analysis for top-down mass spectrometry
Donnelly DP, et al,
Nature Methods, 16(7), 587-594 (2019)
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)

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico