Skip to Content
MilliporeSigma
All Photos(3)

Key Documents

View All Documentation

M6574

Sigma-Aldrich

Membrane Scaffold Protein 1D1

recombinant, expressed in E. coli

Synonym(s):

MSP1D1, MSP1T2

Sign Into View Organizational & Contract Pricing
All Photos(3)

About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

biological source

microbial

Quality Level

200

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

Looking for similar products? Visit Product Comparison Guide

Application

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

Membrane scaffold protein 1D1 (MSP1D1) is derived from apolipoprotein A-I. It is an amphipathic synthetic protein, which self assembles to form nanodiscs.
Generates Nanodiscs ~9.7 nm in diameter

Physical properties

Sequence:GHHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

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

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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)
Synaptosomes (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

Articles

Nanodisc Technology: A Revolutionary System for Study of Membrane Proteins

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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service