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1-萘磷酸双钠盐

1-萘磷酸双钠盐名称

[ CAS 号 ]:
31681-98-8

[ 中文名 ]:
2-萘基磷酸酯二钠盐

[ 英文名 ]:
2-Naphthyl phosphate disodium salt

[中文别名 ]:

1-萘磷酸双钠盐

[英文别名 ]:

2-Naphthalenol,dihydrogenphosphate,d
MFCD00149594
EINECS 250-763-0
2-NAPHTHYL PHOSPHATE DISODIUM SALT
2-NAPHTHYLPHOSPHORIC ACID DISODIUM SALT
Phosphoric acid 2-naphtyldisodium salt
disodium 2-naphthyl phosphate
SODIUM B-NAPHTHYL ACID PHOSPHATE

1-萘磷酸双钠盐物理化学性质

[ 密度 ]:
1.492g/cm3

[ 沸点 ]:
451ºC at 760mmHg

[ 分子式 ]:
C₁₀H₇Na₂O₄P

[ 分子量 ]:
268.11300

[ 闪点 ]:
226.6ºC

[ 精确质量 ]:
267.98800

[ PSA ]:
82.23000

[ LogP ]:
3.18770

[ 外观性状 ]:
白色粉末

[ 储存条件 ]:
−20°C

1-萘磷酸双钠盐安全信息

[ 符号 ]:

GHS07

[ 信号词 ]:
Warning

[ 危害声明 ]:
H315-H319-H335

[ 警示性声明 ]:
P261-P305 + P351 + P338

[ 个人防护装备 ]:
dust mask type N95 (US);Eyeshields;Gloves

[ 危害码 (欧洲) ]:
Xi: Irritant;

[ 风险声明 (欧洲) ]:
36/37/38

[ 安全声明 (欧洲) ]:
26-36

[ 危险品运输编码 ]:
NONH for all modes of transport

[ WGK德国 ]:
3

1-萘磷酸双钠盐文献

Bovine kidney low molecular weight acid phosphatase: FMN-dependent kinetics.

Biochem. Mol. Biol. Int. 41(6) , 1201-8, (1997)

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 w...

Restoration of potent protein-tyrosine phosphatase activity into the membrane-distal domain of receptor protein-tyrosine phosphatase alpha.

Biochemistry 38(3) , 914-22, (1999)

Most transmembrane, receptor-like protein-tyrosine phosphatases (RPTPs) contain two cytoplasmic catalytic protein-tyrosine phosphatase (PTP) domains, of which the membrane-proximal domain, D1, contain...

Inhibition of bovine kidney low molecular mass phosphotyrosine protein phosphatase by uric acid.

J. Enzyme Inhib. Med. Chem. 17(5) , 345-50, (2002)

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...

更多文献

1-萘磷酸双钠盐

1-萘磷酸双钠盐名称

1-萘磷酸双钠盐物理化学性质

1-萘磷酸双钠盐安全信息

1-萘磷酸双钠盐文献

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