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B0184

Bacteriorhodopsin from Halobacterium salinarum

native sequence, lyophilized powder

Synonym(s):

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

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1 mg

Available to ship TODAYfromMILWAUKEE

$1,170.00
5 mg

Available to ship TODAYfromMILWAUKEE

$4,490.00

About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.56
MDL number:
Form:
lyophilized powder
Biological source:
Halobacterium salinarium

$1,170.00


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biological source

Halobacterium salinarium

Quality Level

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.

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M0630P1431H3536
biological source

Halobacterium salinarium

biological source

equine skeletal muscle

biological source

bovine testis

biological source

human plasma (pooled)

technique(s)

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

technique(s)

mass spectrometry (MS): suitable

technique(s)

ligand binding assay: suitable

technique(s)

activity assay: suitable

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

lyophilized powder

form

lyophilized powder

Gene Information

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

Gene Information

horse ... MB(100054434)

Gene Information

cow ... CALM3(520277)

Gene Information

human ... HP(3240)

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

UniProt accession no.

B0R5N9

UniProt accession no.

P68082

UniProt accession no.

P62157

UniProt accession no.

P00738


Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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High production of bacteriorhodopsin from wild type Halobacterium salinarum
Seyedkarimi MS, et al.
Extremophiles : Life Under Extreme Conditions, 19(5), 1021-1028 (2015)
Best practices and benchmarks for intact protein analysis for top-down mass spectrometry
Donnelly DP, et al,
Nature Methods, 16(7), 587-594 (2019)
A review on bacteriorhodopsin-based bioelectronic devices
Li YT, et al.
Sensors, 18(5), 1368-1368 (2018)



Global Trade Item Number

SKUGTIN
B0184-1MG04061833419540
B0184-5MG04061833419557

Questions

1–4 of 4 Questions  
  1. How many liters is the B0184 (Bacteriorhodopsin from Halobacterium salinarum) sample in 1 mg?

    1 answer
    1. 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).

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  2. How many liters is this sample in 1 mg?

    1 answer
    1. 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?

  3. What purification method is utilized in the manufacture of B0184 - Bacteriorhodopsin from Halobacterium salinarum?

    1 answer
    1. 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?

  4. 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
    1. 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%3Dihub

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