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330-13-2

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330-13-2 Usage

Description

P-NITROPHENYL PHOSPHATE DI(TRIS) SALT is a chemical compound that is commonly used as a substrate for the measurement of various enzymatic activities, particularly alkaline phosphatase. It is a colorless compound that, upon hydrolysis, releases a yellow-colored product, making it an ideal choice for colorimetric assays.

Uses

Used in Medical and Diagnostic Applications:
P-NITROPHENYL PHOSPHATE DI(TRIS) SALT is used as a substrate for measuring alkaline phosphatase activity in human serum. The hydrolysis of this compound by alkaline phosphatase releases a yellow-colored product, which can be easily quantified and used to assess the enzyme's activity levels in various medical and diagnostic tests.
Used in Research and Development:
In the field of research and development, P-NITROPHENYL PHOSPHATE DI(TRIS) SALT is utilized as a tool to study the activity and properties of alkaline phosphatase and other related enzymes. P-NITROPHENYL PHOSPHATE DI(TRIS) SALT can be employed in various experimental setups to investigate enzyme kinetics, enzyme inhibition, and enzyme-substrate interactions, contributing to a better understanding of these biological processes.
Used in Quality Control and Validation:
P-NITROPHENYL PHOSPHATE DI(TRIS) SALT is also used in the quality control and validation of alkaline phosphatase assays and other related diagnostic tests. By providing a consistent and reliable substrate for enzyme activity measurement, this compound helps ensure the accuracy and reliability of test results, which is crucial for the proper diagnosis and treatment of various medical conditions.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, P-NITROPHENYL PHOSPHATE DI(TRIS) SALT can be employed in the development and testing of new drugs targeting alkaline phosphatase or related enzymes. By using this compound as a substrate, researchers can evaluate the effectiveness of potential drug candidates and optimize their properties for better therapeutic outcomes.
Overall, P-NITROPHENYL PHOSPHATE DI(TRIS) SALT is a versatile compound with a wide range of applications in various industries, including medical and diagnostic, research and development, quality control, and the pharmaceutical industry. Its ability to serve as a substrate for alkaline phosphatase and other enzymes makes it a valuable tool for measuring enzyme activity, studying enzyme properties, and developing new diagnostic tests and therapeutic agents.

Check Digit Verification of cas no

The CAS Registry Mumber 330-13-2 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 3,3 and 0 respectively; the second part has 2 digits, 1 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 330-13:
(5*3)+(4*3)+(3*0)+(2*1)+(1*3)=32
32 % 10 = 2
So 330-13-2 is a valid CAS Registry Number.
InChI:InChI=1/C6H6NO6P/c8-7(9)5-1-3-6(4-2-5)13-14(10,11)12/h1-4H,(H2,10,11,12)/p-2

330-13-2SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name 4-nitrophenyl phosphate

1.2 Other means of identification

Product number -
Other names Phosphoric acid,mono(4-nitrophenyl) ester

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:330-13-2 SDS

330-13-2Relevant articles and documents

A Protease Mimic with Turnover Capabilities

Menger, F. M.,Whitesell, L. G.

, p. 707 - 708 (1985)

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Effect of hydrophobic interaction cooperating with double Lewis acid activation in a zinc(ii) phosphodiesterase mimic

Zhao, Meng,Zhang, Li,Chen, Huo-Yan,Wang, Han-Lu,Ji, Liang-Nian,Mao, Zong-Wan

, p. 6497 - 6499 (2010)

The novel dinuclear Zn(ii) complex (1) containing a β-CD dimer could accelerate BNPP (a DNA substitute) hydrolysis more efficiently than catalyze HPNP (a RNA substitute) transesterification with different mechanisms involved; the β-CDs played remarkably different roles.

An insight into phosphorylase mechanism from model study

Tafesse, Fikru,Eguzozie, Kennedy

, p. 826 - 830 (2010)

Mechanistic aspects of phosphorylation reaction that mimic phosphorylase enzymes have been studied in the biologically important middle pH region by utilizing nitrophenol as substrate and bistrimethylenediaminecobalt(III) phosphate complexes as the enzyme model. Significant phosphorylation was noted from reactions of 1:1 molar ratio of nitrophenol and bistrimethylenediamincobalt(III) phosphate, [Co(III)tn2Pi]. Enhanced phosphorylation was depicted for reaction solutions that contained 1:1 molar ratio of nitrophenol and di-bistrimethylenediamincobalt(III) phosphate, [(Co(III)tn2)2Pi]. Specific mechanistic features and the possible roles metal ions play in phosphorylase enzyme are highlighted. Copyright Taylor & Francis Group, LLC.

Catalytic zinc complexes for phosphate diester hydrolysis

Tirel, Emmanuel Y.,Bellamy, Zoe,Adams, Harry,Lebrun, Vincent,Duarte, Fernanda,Williams, Nicholas H.

, p. 8246 - 8250 (2014)

Creating efficient artificial catalysts that can compete with biocatalysis has been an enduring challenge which has yet to be met. Reported herein is the synthesis and characterization of a series of zinc complexes designed to catalyze the hydrolysis of phosphate diesters. By introducing a hydrated aldehyde into the ligand we achieve turnover for DNA-like substrates which, combined with ligand methylation, increases reactivity by two orders of magnitude. In contrast to current orthodoxy and mechanistic explanations, we propose a mechanism where the nucleophile is not coordinated to the metal ion, but involves a tautomer with a more effective Lewis acid and more reactive nucleophile. This data suggests a new strategy for creating more efficient metal ion based catalysts, and highlights a possible mode of action for metalloenzymes.

P-nitrophenyl phosphate disodium and preparation method thereof

-

, (2020/01/12)

The invention provides p-nitrophenyl phosphate disodium and a preparation method thereof. The preparation method comprises the following steps: 1, enabling p-nitrophenol to react with dialkyl chloridephosphate in the presence of an alkali so as to obtain O,O-dialkyl p-nitrophenyl phosphate; 2, performing an alkyl ester desorption reaction on the O,O-dialkyl p-nitrophenyl phosphate and a compoundwith trimethylsilyl groups so as to obtain O,O-di(trimethylsilyl) p-nitrophenyl phosphate; 3, performing a hydrolysis reaction on the O,O-di(trimethylsilyl) p-nitrophenyl phosphate so as to obtain p-nitrophenyl phosphate; and 4, enabling the p-nitrophenyl phosphate to react with sodium hydroxide, so as to obtain the p-nitrophenyl phosphate disodium. According to the preparation method provided bythe invention, the intermediate product obtained in the step 1 can be purified through vacuum distillation, and byproducts which are hard to remove are not generated in later operation of ether hydrolysis or pH value adjustment, so that the purification difficulty of the product is greatly reduced; and due to selection of the compound with the trimethylsilyl groups, hydrolysis can be implemented thoroughly, and in addition, the system can be clean.

Characterization of wall teichoic acid degradation by the bacteriophage φ29 appendage protein GP12 using synthetic substrate analogs

Myers, Cullen L.,Ireland, Ronald G.,Garrett, Teresa A.,Brown, Eric D.

, p. 19133 - 19145 (2015/09/08)

Background: The GP12 protein from bacteriophage φ29 is a likely wall teichoic acid hydrolase. Results: GP12 is an efficient catalyst of wall teichoic acid hydrolysis that is influenced by glycosylation of the wall teichioc acid polymer. Conclusion: GP12 m

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