M7074
Membrane Scaffold Protein 1E3D1
recombinant, expressed in E. coli
Synonyme(s) :
MSP1E3D1
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A propos de cet article
NACRES:
NA.26
UNSPSC Code:
12352202
Form:
lyophilized powder
Biological source:
Streptomyces kanamyceticus
Recombinant:
expressed in E. coli
Mol wt:
Mw 32599.98 by amino acid sequence
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Laissez-nous vous aiderbiological source
Streptomyces kanamyceticus
recombinant
expressed in E. coli
description
N-Terminal histidine-tagged
form
lyophilized powder
mol wt
Mw 32599.98 by amino acid sequence
ε (extinction coefficient)
26,600 M-1cm-1 at 280 nm (His-tag-cleaved dissolved in 20 mM Tris pH 7.4, 0.1M NaCl, 0.5mM EDTA and 0.01%NaN3)(lit.), 29,400 M-1cm-1 at 280 nm (uncleaved His-tagged dissolved in 20 mM Tris pH 7.4, 0.1M NaCl, 0.5mM EDTA and 0.01%NaN3)(lit.)
storage temp.
−20°C
Quality Level
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Application
For an extensive list of citations and protocols visit the Sligar Lab Website at; sligarlab.life.uiuc.edu/nanodisc.html
For guidelines on the use of this and other MSP′s to prepare Nanodiscs, please visit our Protocols for Membrane Scaffold Proteins and Nanodisc Formation page.
Nanodisc soluble lipid bilayer systems have proven to be a widely applicable means for rendering membrane proteins soluble in aqueous solutions in a native-like bilayer environment where they remain monodisperse and active. The critical component of nanodiscs is the encircling amphipathic helical protein belt (membrane scaffold protein).
The nanodisc system has been employed to incorporate a wide variety of proteins including GPCRs, P450s, bacteriorhodopsin, coagulation factors, cholera toxin, TAR receptor and aromatase.
Biochem/physiol Actions
Generates Nanodiscs ~12.9 nm in diameter
General description
Sequence: GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
The nanodisc concept is derived from high density lipoprotein (HDL) particles and their primary protein component, apolipoprotein. The nanodisc is a non-covalent structure of phospholipid bilayer and membrane scaffold protein (MSP), a genetically engineered protein, which mimics the function of Apolipoprotein A-1 (ApoA-1). A soluble nanodisc assembles as the phospholipid forms a bilayer, which is encircled by two amphipathic MSP molecules covering the hydrophobic alkyl chains of the bilayer. The length of the MSP controls the size of the nanodisc structure. MSP1E3D1 yields nanodiscs of ~12.9 nm. The thickness of a nanodisc is dependent on the type of phospholipid incorporated (typically 4.6−5.6 nm).
Legal Information
Nanodisc technology, and many of its uses, are covered by the following patents held by the University of Illinois.
- 7,691,414 Membrane scaffold proteins
- 7,662,410 Membrane scaffold proteins and embedded membrane proteins
- 7,622,437 Tissue factor compositions and methods
- 7,592,008 Membrane scaffold proteins
- 7,575,763 Membrane scaffold proteins and tethered membrane proteins
- 7,083,958 Membrane scaffold proteins
- 7,048,949 Membrane scaffold proteins
Physical form
Supplied as a lyophilized histidine-tagged protein with a TEV protease cleavage site stabilized with Tris-HCl, EDTA, and NaCl.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Koichiro E Kishi et al.
Cell, 185(4), 672-689 (2022-02-04)
ChRmine, a recently discovered pump-like cation-conducting channelrhodopsin, exhibits puzzling properties (large photocurrents, red-shifted spectrum, and extreme light sensitivity) that have created new opportunities in optogenetics. ChRmine and its homologs function as ion channels but, by primary sequence, more closely resemble
Mikihiro Shibata et al.
Scientific reports, 8(1), 8262-8262 (2018-05-31)
Oligomeric assembly is a common feature of membrane proteins and often relevant to their physiological functions. Determining the stoichiometry and the oligomeric state of membrane proteins in a lipid bilayer is generally challenging because of their large size, complexity, and
Keiichi Inoue et al.
Nature communications, 7, 13415-13415 (2016-11-18)
Light-driven outward H
Tomomi Shionoya et al.
The journal of physical chemistry. B, 122(27), 6945-6953 (2018-06-13)
Thermophilic rhodopsin (TR) is a light-driven proton pump from the extreme thermophile Thermus thermophilus JL-18. Previous studies on TR solubilized with detergent showed that the protein exhibits high thermal stability and forms a trimer at room temperature but irreversibly dissociates
Tomasz Uchański et al.
Nature methods, 18(1), 60-68 (2021-01-08)
Nanobodies are popular and versatile tools for structural biology. They have a compact single immunoglobulin domain organization, bind target proteins with high affinities while reducing their conformational heterogeneity and stabilize multi-protein complexes. Here we demonstrate that engineered nanobodies can also
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