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Sigma Aldrich Fine Chemicals Biosciences Membrane Scaffold Protein5MG

Catalog No. 502904389
Encompass

Nanodisc technology is an approach to render membrane proteins soluble in aqueous SOLUTIONons 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 MSP1D1 BTN variant of MSP1D1 features an enzymatically biotinylated additional 20-amino acid sequence at the C-terminus of MSP1D1.

Catalog No. 50-290-4389 Supplier Sigma Aldrich Fine Chemicals Biosciences Supplier No. MSP135MG
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Nanodisc technology is an approach to render membrane proteins soluble in aqueous SOLUTIONons 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 MSP1D1 BTN variant of MSP1D1 features an enzymatically biotinylated additional 20-amino acid sequence at the C-terminus of MSP1D1.

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