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Merck
CN

N6005

2-Naphthyl phosphate disodium salt

97%

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About This Item

Linear Formula:
C10H7OP(O)(ONa)2
CAS Number:
31681-98-8
Molecular Weight:
268.11
NACRES:
NA.22
PubChem Substance ID:
24897763
UNSPSC Code:
12352100
EC Number:
250-763-0
MDL number:
MFCD00149594

Key Documents

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Product Name

2-Naphthyl phosphate disodium salt, 97%

InChI

1S/C10H9O4P.2Na.H2O/c11-15(12,13)14-10-6-5-8-3-1-2-4-9(8)7-10;;;/h1-7H,(H2,11,12,13);;;1H2/q;2*+1;/p-2

InChI key

VZEQFWJGQGFKLL-UHFFFAOYSA-L

SMILES string

O.[Na+].[Na+].[O-]P([O-])(=O)Oc1ccc2ccccc2c1

assay

97%

form

powder

storage temp.

−20°C

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Application

2-Naphthyl phosphate disodium salt has been used to study its binding characteristics onto alumina.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
MKCC3479
07302HJ
09220JD
21905PR
11005EN

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Adsorption characteristics of charged and nonionic small molecules to colloidal alumina
Pansare VJ, et al.
Journal of Colloid and Interface Science, 512, 29-38 (2018)
A Buist et al.
Biochemistry, 38(3), 914-922 (1999-01-20)
Most transmembrane, receptor-like protein-tyrosine phosphatases (RPTPs) contain two cytoplasmic catalytic protein-tyrosine phosphatase (PTP) domains, of which the membrane-proximal domain, D1, contains the majority of the activity, while the membrane-distal domain, D2, exhibits little or no activity. We have investigated the
José Mauro Granjeiro et al.
Journal of enzyme inhibition and medicinal chemistry, 17(5), 345-350 (2003-04-10)
Uric acid inhibited 50% of the activity of bovine kidney low molecular mass phosphotyrosine protein phosphatase at concentrations of 1.0, 0.4, 1.3, and 0.2 mM, respectively for p-nitrophenyl phosphate (p-NPP), flavine mononucleotide, beta-naphthyl phosphate and tyrosine phosphate (Tyr-P) as substrates.
C Hipólito-Reis et al.
Scandinavian journal of clinical and laboratory investigation, 59(8), 593-606 (2000-02-26)
The importance of separation and identification of serum alkaline phosphatase (ALP; E.C. 3.1.3.1) fractions/isoenzymes has been frequently reported. Each serum ALP fraction/isoenzyme quantitation has both practical and theoretical importance. In the present work, serum was collected from Wistar rats and
J M Granjeiro et al.
Biochemistry and molecular biology international, 41(6), 1201-1208 (1997-05-01)
A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0.

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