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Merck

M7074

Sigma-Aldrich

Membrane Scaffold Protein 1E3D1

recombinant, expressed in E. coli

Szinonimák:

MSP1E3D1

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352202
NACRES:
NA.26

biológiai forrás

Streptomyces kanamyceticus

Minőségi szint

rekombináns

expressed in E. coli

leírás

N-Terminal histidine-tagged

form

lyophilized powder

molekulatömeg

Mw 32599.98 by amino acid sequence

ε (extinkciós együttható)

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.)

tárolási hőmérséklet

−20°C

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Általános leírás

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).

Alkalmazás

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.

Biokémiai/fiziológiai hatások

Generates Nanodiscs ~12.9 nm in diameter

Fizikai tulajdonságok

Sequence: GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

Fizikai forma

Supplied as a lyophilized histidine-tagged protein with a TEV protease cleavage site stabilized with Tris-HCl, EDTA, and NaCl.

Jogi információk

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

Piktogramok

Exclamation mark

Figyelmeztetés

Warning

Figyelmeztető mondatok

Óvintézkedésre vonatkozó mondatok

Veszélyességi osztályok

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Célzott szervek

Respiratory system

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
Keiichi Inoue et al.
Nature communications, 7, 13415-13415 (2016-11-18)
Light-driven outward H
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
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.
Science advances, 6(15), eaaz2441-eaaz2441 (2020-04-18)
Schizorhodopsins (SzRs), a rhodopsin family first identified in Asgard archaea, the archaeal group closest to eukaryotes, are present at a phylogenetically intermediate position between typical microbial rhodopsins and heliorhodopsins. However, the biological function and molecular properties of SzRs have not

Cikkek

Read our article about how the Nanodisc system allows for structural studies of membrane proteins.

Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.

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