This product is sold as a lyophilized powder. The method of preparation is described in "Methods in Enzymology" by Oesterhelt, D., and Stoeckenius, W., titled "Isolation of the cell membrane of Halobacterium halobium and 1st fractionation into red and purple membrane," published in Meth. Enzymol., 31, 667-678 (1974).
B0184
Bacteriorhodopsin from Halobacterium salinarum
native sequence, lyophilized powder
Sinonimo/i:
BR from H. salinarum, Bacterioopsin, Bacteriorhodopsin from Halobacterium halobium
Autenticati per visualizzare i prezzi organizzativi e contrattuali.
Scegli un formato
Cambia visualizzazione
| Voi/SKU | Disponibilità | Prezzo |
|---|---|---|
1 mg | Per conoscere la disponibilità, visualizza il carrello | CHF 804.00 |
5 mg | Per conoscere la disponibilità, visualizza il carrello | CHF 3220.00 |
Informazioni su questo articolo
Form:
lyophilized powder
Biological source:
Halobacterium salinarium
CHF 804.00
Per conoscere la disponibilità, visualizza il carrello
Servizio Tecnico
Hai bisogno di aiuto? Il nostro team di scienziati qualificati è a tua disposizione.
Permettici di aiutartibiological source
Halobacterium salinarium
Quality Segment
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)
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.
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.
Application
Bacteriorhodopsin is of interest in the development of artificial retinas, optical associative processors, and three-dimensional memory storage devices.
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
Biochem/physiol Actions
A transmembrane retinylidine protein that functions as a proton pump driven by light energy in Holobacterium.
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.
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.
1 of 1
Questo articolo | |||
|---|---|---|---|
| description native sequence, lyophilized powder | description ≥95% (SDS-PAGE), lyophilized powder | description lyophilized powder | description ≥99% |
| biological source Halobacterium salinarium | biological source human plasma (pooled) | biological source bovine serum (fetal) | biological source bovine plasma |
| technique(s) mass spectrometry (MS): suitable, ligand binding assay: suitable | technique(s) activity assay: suitable | technique(s) HPLC: suitable, MALDI-MS: suitable | technique(s) mass spectrometry (MS): suitable, electrophoresis: suitable |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form powder |
| storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C |
| Gene Information Halobacterium salinarium ... OE_RS05715(5953595), VNG_RS05715(144807) | Gene Information human ... HP(3240) | Gene Information bovine ... FETUB(504615) | Gene Information bovine ... ORM1(497200) |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. |
Classe di stoccaggio
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
-
How many liters is the B0184 (Bacteriorhodopsin from Halobacterium salinarum) sample in 1 mg?
1 answer-
Helpful?
-
-
How many liters is this sample in 1 mg?
1 answer-
This product is a lyophilized powder offered in 1 milligram and 5 milligram quantities. The material is not available in liter quantities or volumes.
Helpful?
-
-
What purification method is utilized in the manufacture of B0184 - Bacteriorhodopsin from Halobacterium salinarum?
1 answer-
The preparation method is based on the description provided in Methods in Enzymology by Oesterhelt, D., and Stoeckenius, W. The specific article is titled "Isolation of the cell membrane of Halobacterium halobium and 1st fractionation into red and purple membrane" and is published in Meth. Enzymol., 31, 667-678 (1974).
Helpful?
-
-
I would like to know more details on how B0184 (Bacteriorhodopsin from Halobacterium salinarum) was prepared, isolated, and purified. We are preparing a publication that describes the analysis of this product, and we need this information for the paper.
1 answer-
The method of preparation is essentially that described in Methods in Enzymology. Oesterhelt, D., and Stoeckenius, W., "Isolation of the cell membrane of Halobacterium halobium and 1st fractionation into red and purple membrane.", Meth. Enzymol., 31, 667-678 (1974).
https://pubmed.ncbi.nlm.nih.gov/4418026/
https://www.sciencedirect.com/science/article/pii/0076687974310725?via%3DihubHelpful?
-