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M7074

Membrane Scaffold Protein 1E3D1

recombinant, expressed in E. coli

Synonyma:

MSP1E3D1

Přihlásit pro zobrazení organizačních a smluvních cen.

Vybrat velikost

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Velikost baleníSkladová položkaDostupnostCena
5 mg
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13 400,00 Kč

O této položce

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

13 400,00 Kč


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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

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).

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

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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Tato položka
MSP04M6574MSP03
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

biological source

Streptomyces kanamyceticus

biological source

-

biological source

microbial

biological source

-

mol wt

Mw 32599.98 by amino acid sequence

mol wt

-

mol wt

Mw 24661.9 by amino acid sequence

mol wt

22,043.9 Da

form

lyophilized powder

form

buffered aqueous solution

form

lyophilized powder

form

buffered aqueous solution

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


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pictograms

Exclamation mark

signalword

Warning

Hazard Classifications

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

target_organs

Respiratory system

Skladovací třída

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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Související obsah

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


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
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



Globální číslo obchodní položky

Skladová položkaGTIN
M7074-5MG04061834061601

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