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모든 사진(3)

Key Documents

M7074

Sigma-Aldrich

Membrane Scaffold Protein 1E3D1

recombinant, expressed in E. coli

동의어(들):

MSP1E3D1

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About This Item

UNSPSC 코드:
12352202
NACRES:
NA.26

생물학적 소스

Streptomyces kanamyceticus

Quality Level

재조합

expressed in E. coli

설명

N-Terminal histidine-tagged

형태

lyophilized powder

분자량

Mw 32599.98 by amino acid sequence

ε (흡광계수)

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.)

저장 온도

−20°C

유사한 제품을 찾으십니까? 방문 제품 비교 안내

일반 설명

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).

애플리케이션

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.

생화학적/생리학적 작용

Generates Nanodiscs ~12.9 nm in diameter

물리적 특성

Sequence: GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

물리적 형태

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

법적 정보

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

픽토그램

Exclamation mark

신호어

Warning

유해 및 위험 성명서

예방조치 성명서

Hazard Classifications

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

표적 기관

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

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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
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

문서

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

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