MSP09
Membrane Scaffold Protein 1E3D1 D73C
recombinant, expressed in E. coli, Cysteine substituted at position 73
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About This Item
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recombinant
expressed in E. coli
Quality Level
assay
≥90% (SDS-GE)
form
buffered aqueous solution
shipped in
ambient
storage temp.
−20°C
General description
Nanodisc technology is an approach to render membrane proteins soluble in aqueous solutions in a native-like bilayer environment, where the membrane proteins remain stable and active. 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).
The first MSP, MSP1, was engineered with its sequence based on the sequence of A-1, but without the globular N-terminal domain of native A-1. The MSP1E3D1 D73C variant of MSP1 differs from MSP1 in the following facets:
The first MSP, MSP1, was engineered with its sequence based on the sequence of A-1, but without the globular N-terminal domain of native A-1. The MSP1E3D1 D73C variant of MSP1 differs from MSP1 in the following facets:
- It deletes the first 11 amino acids in the Helix 1 portion (referred to as “H0.5” in the accompanying figure) of the original MSP1 sequence3 (which is known separately as MSP1D1).
- It repeats the Helix 4 (H4), Helix 5 (H5) and Helix 6 (H6) sequences of the original MSP1 sequence between the parent Helix 6 (H6) and Helix 7 (H7) segments of MSP1D1.
- It substitutes a cysteine (C) residue for an aspartic acid (D) residue in the Helix 2 (H2) portion of the protein, at position 73 of the original native A-1 sequence.
- The initial histidine-tag is one amino acid shorter.
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.
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
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Protocols
Nanodisc technology aids membrane protein solubilization, overcoming associated challenges in diverse protein classes.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
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