recombinant
expressed in E. coli
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 Membrane Scaffold Protein 1D1 (MSP1D1) variant of MSP1 deletes the first 11 amino acids in the Helix 1 portion (referred to as “H0.5” in the accompanying figure) of the original MSP1 sequence. The MSP1ΔW variant of MSP1D1, sometimes referred to as “Dark MSP”, replaces the two tryptophan (W) residues in the parent MSP1D1 sequence with phenylalanines (F). These two (W→F) substitutions are at the following positions of the original native A-1 sequence:
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 Membrane Scaffold Protein 1D1 (MSP1D1) variant of MSP1 deletes the first 11 amino acids in the Helix 1 portion (referred to as “H0.5” in the accompanying figure) of the original MSP1 sequence. The MSP1ΔW variant of MSP1D1, sometimes referred to as “Dark MSP”, replaces the two tryptophan (W) residues in the parent MSP1D1 sequence with phenylalanines (F). These two (W→F) substitutions are at the following positions of the original native A-1 sequence:
- Position 72, within the Helix 2 (H2) segment
- Position 108, within the Helix 4 (H4) segment
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
存儲類別/等級
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
條款
The following material related to Nanodisc Technology is adapted from on-line content of the research group of Professor Stephen Sligar of the University of Illinois at Urbana-Champaign, with the kind permission of Professor Sligar.
Nanodisc technology aids membrane protein solubilization, overcoming associated challenges in diverse protein classes.
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