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MDR-1 (human) full length protein-synthetic nanodisc
Product information "MDR-1 (human) full length protein-synthetic nanodisc"
Discover a breakthrough in membrane protein research and drug development with DIMA Biotech's Synthetic Nanodiscs. Traditional methods struggle with challenges in obtaining water-soluble and bioactive forms of multi-transmembrane proteins. Our innovative polymer-based Nanodisc platform offers a game-changing solution by excluding membrane scaffold proteins (MSPs), resulting in a cleaner system with fewer interferences for downstream assays. By disassembling cell membranes into nanoscale disc-shaped structures, our technology enables the purification of membrane proteins to high homogeneity under aqueous conditions. Explore how Synthetic Nanodiscs empower the functional characterization of multi-span transmembrane proteins in their active form, revolutionizing the future of membrane protein research and drug development. Protein function: Translocates drugs and phospholipids across the membrane (PubMed:8898203, PubMed:2897240, PubMed:9038218). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:2897240, PubMed:9038218). [The UniProt Consortium]
Keywords:
MDR1, CD243, EC=7.6.2.2, P-glycoprotein 1, Phospholipid transporter ABCB1, Multidrug resistance protein 1, ATP-dependent translocase ABCB1, ATP-binding cassette sub-family B member 1, ABCB1, CD243, CLCS, GP170, MDR1, p-170, P-GP, PGY1, Human MDR-1
This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the usability of this website, serve for direct advertising or simplify interaction with other websites and social networks, will only be used with your consent.
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