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N5885

4-Nitrophenyl α-D-maltoside

Name: 4-Nitrophenyl α-<SC>D</SC>-maltoside
Brand: SIGMA

glycosidase substrate

Synonym(s):

4-Nitrophenyl a-D-maltopyranoside, 4-Nitrophenyl alpha-D-maltoside

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About This Item

Empirical Formula (Hill Notation):

C₁₈H₂₅NO₁₃

CAS Number:

17400-77-0

Molecular Weight:

463.39

NACRES:

NA.32

PubChem Substance ID:

24897757

UNSPSC Code:

12352204

MDL number:

MFCD00036769

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Properties

Quality Level

200

assay

≥99% (TLC)

form

powder

solubility

water: 49.00-51.00 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

SMILES string

O[C@@H]1[C@@H](O)[C@H](O[C@@]2([H])O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](CO)O[C@@H]1OC3=CC=C([N+]([O-])=O)C=C3

InChI

1S/C18H25NO13/c20-5-9-11(22)12(23)14(25)18(30-9)32-16-10(6-21)31-17(15(26)13(16)24)29-8-3-1-7(2-4-8)19(27)28/h1-4,9-18,20-26H,5-6H2

InChI key

IAYJZWFYUSNIPN-UHFFFAOYSA-N

Description

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number

0000560619

0000479747

117M4036V

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Transport of p-nitrophenyl-alpha-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic alpha-maltosidase.

M Reyes et al.

Journal of bacteriology, 165(3), 918-922 (1986-03-01)

In wild-type Escherichia coli the activity of the maltose transport system is dependent on a periplasmic maltose-binding protein. It has been possible, however, to isolate mutants in which transport activity is mediated by the membrane components of the system and

Effect of a p-nitro group of phenyl-maltooligosaccharide substrate on the change of action specificity of lysine-modified porcine pancreatic alpha-amylase.

H Yamashita et al.

Biochemistry and molecular biology international, 35(1), 79-85 (1995-01-01)

The effect of chemical modification of lysine residues on the activity of porcine pancreatic alpha-amylase (PPA) was examined, using p-nitrophenyl-alpha-D-maltoside, p-nitrophenyl-alpha-D-maltotrioside, phenyl-alpha-D-maltoside and phenyl-alpha-D-maltotrioside as substrates. Chemical modification of PPA with trinitrobenzenesulfonic acid enhanced the kcat/Km values for p-nitrophenyl substrates

Barley malt-alpha-amylase. Purification, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates.

E H Ajandouz et al.

Biochimica et biophysica acta, 1159(2), 193-202 (1992-09-23)

Isoforms AMY1, AMY2-1 and AMY2-2 of barley alpha-amylase were purified from malt. AMY2-1 and AMY2-2 are both susceptible to barley alpha-amylase/subtilisin inhibitor. The action of these isoforms is compared using substrates ranging from p-nitrophenylmaltoside through p-nitrophenylmaltoheptaoside. The kcat/Km values are

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Global Trade Item Number

SKU	GTIN
N5885-100MG	04061834117254