850336 | MAPCHO™-12
n-dodecylphosphocholine

MAPCHO™-12
n-dodecylphosphocholine
MAPCHO™-12, or n-dodecyl-β-D-maltopyranoside, is a zwitterionic detergent designed for the efficient solubilization, stabilization, and structural analysis of membrane proteins. It features a 12-carbon dodecyl chain linked to a phosphocholine headgroup and closely mimics the natural lipid environment of biological membranes.
With a critical micelle concentration (CMC) of approximately 1.5 mM, MAPCHO™-12 forms highly stable micelles and offers a mild but effective solubilization environment. It also prevents denaturation and aggregation to ensure proteins remain functional throughout experimentation.
Application
MAPCHO™-12 facilitates the extraction, stabilization, and functional study of transmembrane proteins, including GPCRs, ion channels, and transporters—all essential for drug discovery and biochemical research. Its ability to help in the determination of membrane protein conformations and interactions makes it a go-to detergent for high-resolution structural studies.
Another notable characteristic of MAPCHO™-12 is its ability to support the formation of proteoliposomes, membrane mimetics, and lipid-protein interaction assays. This enables researchers to study biological membranes in a controlled setting. It is also used in drug discovery, receptor-ligand interaction analysis, and detergent screening to optimize protein formulations for therapeutic development.
Packaging
Avanti Research™ provides MAPCHO™-12 in powder (1g, 5g, and 25g), offering flexible options to meet diverse research and formulation needs.
With over 50 years of expertise in lipid and detergent innovation, Avanti ensures the highest purity and consistency, supporting those involved in groundbreaking research and development.
CAS Registry Number is a Registered Trademark of the American Chemical Society
Fos-Choline12
FOS12
FC-12
770336
Santisteban NP, Morrow MR, Booth V. Effect of AMPs MSI-78 and BP100 on the lipid acyl chains of 2H-labeled intact Gram positive bacteria. Biochim Biophys Acta Biomembr. 2020 Jan 25;1862(5):183199. doi: 10.1016/j.bbamem.2020.183199. Epub ahead of print. PMID: 31987866.
PubMed ID: 31987866Liu N, Girvin ME, Brenowitz M, Lai JR. Conformational and lipid bilayer-perturbing properties of Marburg virus GP2 segments containing the fusion loop and membrane-proximal external region/transmembrane domain. Heliyon. 2019 Dec 12;5(12):e03018. doi: 10.1016/j.heliyon.2019.e03018. PMID: 31890962; PMCID: PMC6926192.
PubMed ID: 31890962Mark A. Strege, Siyuan Huang & Donald S. Risley. Quantitative determination of beta-cyclodextrin in a powder insulin formulation for nasal delivery using hydrophilic interaction chromatography with evaporative light scattering detection. Journal of Liquid Chromatography & Related Technologies. 2019 March 25;42(3-4):74-78. doi: 10.1080/10826076.2019.1571508
Abd Rahim MS, Cherniavskyi YK, Tieleman DP, Dames SA. NMR- and MD simulation-based structural characterization of the membrane-associating FATC domain of ataxia telangiectasia mutated. J Biol Chem. 2019 Mar 13. pii: jbc.RA119.007653. doi: 10.1074/jbc.RA119.007653. [Epub ahead of print]
PubMed ID: 30867195Keceli G, Majumdar A, Thorpe CN, Jun S, Tocchetti CG, Lee DI, Mahaney JE, Paolocci N, Toscano JP. Nitroxyl (HNO) targets phospholamban cysteines 41 and 46 to enhance cardiac function. J Gen Physiol. 2019 Mar 6. pii: jgp.201812208. doi: 10.1085/jgp.201812208. [Epub ahead of print]
PubMed ID: 30842219Frey L, Hiller S, Riek R, Bibow S. Lipid- and Cholesterol-Mediated Time-Scale-Specific Modulation of the Outer Membrane Protein X Dynamics in Lipid Bilayers. J Am Chem Soc. 2018 Oct 23. doi: 10.1021/jacs.8b09188. [Epub ahead of print]
PubMed ID: 30289706 Bao H, Goldschen-Ohm M, Jeggle P, Chanda B, Edwardson JM, Chapman ER. Exocytotic fusion pores are composed of both lipids and proteins. Nat Struct Mol Biol. 2016 Jan;23(1):67-73. doi: 10.1038/nsmb.3141. Epub 2015 Dec 14.
PubMed ID: 26656855Palladino, P., Rossi, F., Ragone, R. (2010) Effective critical micellar concentration of a zwitterionic detergent: a fluorimetric study on n-dodecyl phosphocholine. J Fluoresc. 20:191-6.
PubMed ID: 19756982Liang, B., Tamm, L.K. (2007) Structure of outer membrane protein G by solution NMR spectroscopy. Proc Natl Acad Sci U S A. 104:16140-5.
PubMed ID: 17911261Brunecky, R., Lee, S., Rzepecki, P.W., Overduin, M., Prestwich, G.D., Kutateladze, A.G., Kutateladze, T.G. (2005) Investigation of the binding geometry of a peripheral membrane protein. Biochemistry. 44:16064-71.
PubMed ID: 16331966Liu, D.Z., LeCluyse, E.L., Thakker, D.R. (1999) Dodecylphosphocholine-mediated enhancement of paracellular permeability and cytotoxicity in Caco-2 cell monolayers. J Pharm Sci. 88:1161-8.
PubMed ID: 10564065Vasudevan, S.V., Schulz, J., Zhou, C., Cocco, M.J. (2010) Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. Proc Natl Acad Sci U S A. 2010 Apr 13;107(15):6847-51. doi: 10.1073/pnas.0911817107. Epub 2010 Mar 29.
PubMed ID: 20351248- Certificate of Analysis (Lot No. 850336P-1G-A-071 and 5639PQA071)
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