M7074
Membrane Scaffold Protein 1E3D1
recombinant, expressed in E. coli
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All Photos(3)
Synonym(s):
MSP1E3D1
UNSPSC Code:
12352202
NACRES:
NA.26
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biological source
Streptomyces kanamyceticus
Quality Level
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
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General description
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).
Application
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.
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.
Biochem/physiol Actions
Generates Nanodiscs ~12.9 nm in diameter
Physical properties
Sequence: GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
Physical form
Supplied as a lyophilized histidine-tagged protein with a TEV protease cleavage site stabilized with Tris-HCl, EDTA, and NaCl.
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
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Product No.
Description
Pricing
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
Wataru Shihoya et al.
Nature, 574(7776), 132-136 (2019-09-27)
Heliorhodopsins (HeRs) are a family of rhodopsins that was recently discovered using functional metagenomics1. They are widely present in bacteria, archaea, algae and algal viruses2,3. Although HeRs have seven predicted transmembrane helices and an all-trans retinal chromophore as in the
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
Keiichi Inoue et al.
Nature communications, 7, 13415-13415 (2016-11-18)
Light-driven outward H
Articles
Read our article about how the Nanodisc system allows for structural studies of membrane proteins.
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