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D5172

Sigma-Aldrich

n-Dodecyl β-D-maltoside

BioXtra, ≥98% (GC)

Synonym(s):

DDM, Lauryl-β-D-maltoside

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About This Item

Empirical Formula (Hill Notation):
C24H46O11
CAS Number:
Molecular Weight:
510.62
Beilstein/REAXYS Number:
55318
MDL number:
UNSPSC Code:
12161900
eCl@ss:
32190102
PubChem Substance ID:
NACRES:
NA.25

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description

non-ionic

Quality Level

product line

BioXtra

assay

≥98% (GC)

form

powder

mol wt

micellar avg mol wt 50,000

aggregation number

98

technique(s)

protein purification: suitable
protein quantification: suitable

impurities

≤0.0005% Phosphorus (P)
≤0.1% Insoluble matter

ign. residue

≤0.1%

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1 of 4

This Item
D4641324355D7658
form

powder

form

powder

form

solid

form

powder

technique(s)

protein purification: suitable, protein quantification: suitable

technique(s)

protein quantification: suitable

technique(s)

-

technique(s)

-

assay

≥98% (GC)

assay

≥98% (GC)

assay

≥98% (HPLC)

assay

≥98% (GC)

aggregation number

98

aggregation number

98

aggregation number

98

aggregation number

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

mol wt

micellar avg mol wt 50,000

mol wt

micellar avg mol wt 50,000

mol wt

micellar wt 50000

mol wt

482.56 g/mol

General description

n-Dodecyl β-D-maltoside is a non-ionic surfactant belonging to the alkyl polyglucoside family. [1]

Application

Non-ionic detergent for the stabilization and activation of enzymes and for membrane research.
Non-ionic detergent used to extract and solubilize proteins.
n-Dodecyl β-D-maltoside has been used in a study to assess the effect of detergents on the thermal behavior of elastin-like polypeptides (ELP). [2] It has also been used in a study to investigate how membrane structures will respond to detergent solubilization from amino acid sequences. [3]

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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    Rotational Diffusion of Coumarin 153 in Nanoscopic Micellar Environments of n-dodecyl-β-D-maltoside and n-dodecyl-hexaethylene-glycol Mixtures
    Hierrezuelo, H. and C. Ruiz
    The Journal of Physical Chemistry, 116, 12476-12476 (2012)
    Effect of detergents on the thermal behavior of elastin-like polypeptides
    Thapa, A.
    Biopolymers, 99, 55-55 (2012)
    Antonello Calcutta et al.
    Biochimica et biophysica acta, 1818(9), 2290-2301 (2012-04-25)
    Membrane proteins are vital for biological function, and their action is governed by structural properties critically depending on their interactions with the membranes. This has motivated considerable interest in studies of membrane protein folding and unfolding. Here the structural changes
    Vincent G Nadeau et al.
    Biochemistry, 51(31), 6228-6237 (2012-07-12)
    The ability to predict from amino acid sequence how membrane protein structures will respond to detergent solubilization would significantly facilitate experimental characterization of these molecules. Here we have investigated and compared the response to solubilization by the "mild" n-dodecyl-β-D-maltoside (DDM)
    Stephen B Long et al.
    Science (New York, N.Y.), 309(5736), 897-903 (2005-07-09)
    Voltage-dependent potassium ion (K+) channels (Kv channels) conduct K+ ions across the cell membrane in response to changes in the membrane voltage, thereby regulating neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal

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