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Merck

M6574

Membrane Scaffold Protein 1D1

recombinant, expressed in E. coli

Sinónimos:

MSP1D1, MSP1T2

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NACRES:
NA.26
UNSPSC Code:
12352202
Form:
lyophilized powder
Biological source:
microbial
Recombinant:
expressed in E. coli
Mol wt:
Mw 24661.9 by amino acid sequence

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Nombre del producto

Membrane Scaffold Protein 1D1, recombinant, expressed in E. coli

biological source

microbial

recombinant

expressed in E. coli

description

N-Terminal histidine-tagged

form

lyophilized powder

mol wt

Mw 24661.9 by amino acid sequence

ε (extinction coefficient)

18200 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.)
21000 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

200

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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.
Membrane Scaffold Protein 1D1 has been used as a scaffolding protein to stabilize lipid nanodiscs (NDs). It has also been used for the preparation of nanodiscs.
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 ~9.7 nm in diameter
Membrane scaffold protein 1D1 (MSP1D1) is derived from apolipoprotein A-I. It is an amphipathic synthetic protein, which self assembles to form nanodiscs.

General description

Sequence:GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

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.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

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

target_organs

Respiratory system

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
0000517464
0000517464
0000479517
0000479517
0000479516

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Synaptosomes (2018)
Lipid nanotechnologies for structural studies of membrane-associated proteins
Stoilova-McPhie S, et al.
Proteins: Structure, Function, and Bioinformatics, 82(11), 2902-2909 (2014)
Lipid nanotechnologies for structural studies of membrane-associated proteins.
Stoilova-McPhie, S., et al.
Proteins: Structure, Function, and Genetics, 82(11), 2902-2909 (2014)
Time-course and degradation rate of membrane scaffold protein (MSP1D1) during recombinant production
Faas R, et al.
Biotechnology reports (Amsterdam, Netherlands), 17, 45-48 (2018)
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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