N2127
4-Nitrophenyl α-D-mannopyranoside
α-mannosidase substrate, chromogenic, ≥98% (TLC), powder
Synonym(s):
4-Nitrophenyl a-D-mannopyranoside, 4-Nitrophenyl alpha-D-mannopyranoside, pNP-alpha-D-Man, pNPalphaMan
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About This Item
Empirical Formula (Hill Notation):
C12H15NO8
CAS Number:
Molecular Weight:
301.25
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
EC Number:
233-776-6
MDL number:
Beilstein/REAXYS Number:
92210
Product Name
4-Nitrophenyl α-D-mannopyranoside, α-mannosidase substrate
Quality Level
assay
≥98% (TLC)
form
powder
solubility
DMF: 50 mg/mL
storage temp.
−20°C
SMILES string
OC[C@H]1O[C@H](Oc2ccc(cc2)[N+]([O-])=O)[C@@H](O)[C@@H](O)[C@@H]1O
InChI
1S/C12H15NO8/c14-5-8-9(15)10(16)11(17)12(21-8)20-7-3-1-6(2-4-7)13(18)19/h1-4,8-12,14-17H,5H2/t8-,9-,10+,11+,12+/m1/s1
InChI key
IFBHRQDFSNCLOZ-GCHJQGSQSA-N
General description
4-Nitrophenyl α-D-mannopyranoside is a chromogenic substrate for α-mannosidase.
Application
4-Nitrophenyl α-D-mannopyranoside has been used as a substrate for α-mannosidase in hydrolase activity assay.
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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Daniel J Coleman et al.
Analytical biochemistry, 399(1), 7-12 (2009-12-23)
A simple and reliable continuous assay for measurement of alpha-mannosidase activity is described and demonstrated for analysis with two recombinant human enzymes using the new substrate resorufin alpha-d-mannopyranoside (Res-Man). The product of enzyme reaction, resorufin, exhibits fluorescence emission at 585
P N Kanellopoulos et al.
Journal of structural biology, 116(3), 345-355 (1996-05-01)
Concanavalin A (Con A) is the best-known plant lectin and has important in vitro biological activities arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complexes of Con A with 4'-nitrophenyl-alpha-D-mannopyranoside (alpha-PNM) and 4'-nitrophenyl-alpha-D-glucopyranoside (alpha-PNG)
S Jelinek-Kelly et al.
The Journal of biological chemistry, 260(4), 2253-2257 (1985-02-25)
Fractionation of a crude extract from Saccharomyces cerevisiae X-2180 on Sepharose 6B in the presence of 0.5% Triton X-100 resolves two enzyme fractions containing alpha-mannosidase activity. Fraction I which is excluded from the gel contains alpha-mannosidase activity toward both p-nitrophenyl-alpha-D-mannopyranoside