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696-07-1

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696-07-1 Usage

Chemical Properties

white to light yellow fluffy powder

Uses

Different sources of media describe the Uses of 696-07-1 differently. You can refer to the following data:
1. 5-Iodouracil is a halogenated pyrimidine that can be used in nucleoprotein photo-crosslinking via RNA substitution. 5-Iodouracil is used in thymidine phosphorylase targeted imaging and therapy. Studie s show that DNA N-glycosylase MED1 exhibited higher preference for 5-Iodouracil and halogenated bases over non-halogenated ones.
2. 5-Iodouracil is a halogenated pyrimidine that can be used in nucleoprotein photo-crosslinking via RNA substitution. 5-Iodouracil is used in thymidine phosphorylase targeted imaging and therapy. Studies show that DNA N-glycosylase MED1 exhibited higher preference for 5-Iodouracil and halogenated bases over non-halogenated ones.

Definition

ChEBI: An organoiodine compound consisting of uracil having an iodo substituent at the 5-position.

Check Digit Verification of cas no

The CAS Registry Mumber 696-07-1 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 6,9 and 6 respectively; the second part has 2 digits, 0 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 696-07:
(5*6)+(4*9)+(3*6)+(2*0)+(1*7)=91
91 % 10 = 1
So 696-07-1 is a valid CAS Registry Number.
InChI:InChI=1/C4H3IN2O2/c5-2-1-6-4(9)7-3(2)8/h1H,(H2,6,7,8,9)

696-07-1 Well-known Company Product Price

  • Brand
  • (Code)Product description
  • CAS number
  • Packaging
  • Price
  • Detail
  • TCI America

  • (I0219)  5-Iodouracil  >99.0%(HPLC)(T)

  • 696-07-1

  • 5g

  • 235.00CNY

  • Detail
  • TCI America

  • (I0219)  5-Iodouracil  >99.0%(HPLC)(T)

  • 696-07-1

  • 25g

  • 650.00CNY

  • Detail
  • Alfa Aesar

  • (A18994)  5-Iodouracil, 97%   

  • 696-07-1

  • 10g

  • 410.0CNY

  • Detail
  • Alfa Aesar

  • (A18994)  5-Iodouracil, 97%   

  • 696-07-1

  • 50g

  • 1682.0CNY

  • Detail
  • Alfa Aesar

  • (A18994)  5-Iodouracil, 97%   

  • 696-07-1

  • 250g

  • 7378.0CNY

  • Detail
  • Aldrich

  • (857858)  5-Iodouracil  98%

  • 696-07-1

  • 857858-10G

  • 920.79CNY

  • Detail

696-07-1SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name 5-iodouracil

1.2 Other means of identification

Product number -
Other names 5-iodopyriMidine-2.4-diol

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:696-07-1 SDS

696-07-1Relevant articles and documents

Electrochemical Synthesis of 5-Selenouracil Derivatives by Selenylation of Uracils

Chen, Yan-Yan,Jiang, Cai-Na,Ma, Xian-Li,Wang, Qian,Xu, Yan-Li

, (2020)

A simple and efficient electrochemical selenylation of uracils in the presence of NH4I for the synthesis of 5-selenouracils has been developed. This transformation was performed in the transition metal-free, oxidant-free, and aerobic conditions, providing a rapid and practical protocol to 5-selenouracil derivatives.

Thermodynamic Reaction Control of Nucleoside Phosphorolysis

Kaspar, Felix,Giessmann, Robert T.,Neubauer, Peter,Wagner, Anke,Gimpel, Matthias

supporting information, p. 867 - 876 (2020/01/24)

Nucleoside analogs represent a class of important drugs for cancer and antiviral treatments. Nucleoside phosphorylases (NPases) catalyze the phosphorolysis of nucleosides and are widely employed for the synthesis of pentose-1-phosphates and nucleoside analogs, which are difficult to access via conventional synthetic methods. However, for the vast majority of nucleosides, it has been observed that either no or incomplete conversion of the starting materials is achieved in NPase-catalyzed reactions. For some substrates, it has been shown that these reactions are reversible equilibrium reactions that adhere to the law of mass action. In this contribution, we broadly demonstrate that nucleoside phosphorolysis is a thermodynamically controlled endothermic reaction that proceeds to a reaction equilibrium dictated by the substrate-specific equilibrium constant of phosphorolysis, irrespective of the type or amount of NPase used, as shown by several examples. Furthermore, we explored the temperature-dependency of nucleoside phosphorolysis equilibrium states and provide the apparent transformed reaction enthalpy and apparent transformed reaction entropy for 24 nucleosides, confirming that these conversions are thermodynamically controlled endothermic reactions. This data allows calculation of the Gibbs free energy and, consequently, the equilibrium constant of phosphorolysis at any given reaction temperature. Overall, our investigations revealed that pyrimidine nucleosides are generally more susceptible to phosphorolysis than purine nucleosides. The data disclosed in this work allow the accurate prediction of phosphorolysis or transglycosylation yields for a range of pyrimidine and purine nucleosides and thus serve to empower further research in the field of nucleoside biocatalysis. (Figure presented.).

Mtb PKNA/PKNB Dual Inhibition Provides Selectivity Advantages for Inhibitor Design to Minimize Host Kinase Interactions

Wang, Tiansheng,Bemis, Guy,Hanzelka, Brian,Zuccola, Harmon,Wynn, Michael,Moody, Cameron Stuver,Green, Jeremy,Locher, Christopher,Liu, Aixiang,Gao, Hongwu,Xu, Yuzhou,Wang, Shaohui,Wang, Jie,Bennani, Youssef L.,Thomson, John A.,Müh, Ute

supporting information, p. 1224 - 1229 (2017/12/26)

Drug resistant tuberculosis (TB) infections are on the rise and antibiotics that inhibit Mycobacterium tuberculosis through a novel mechanism could be an important component of evolving TB therapy. Protein kinase A (PknA) and protein kinase B (PknB) are both essential serine-threonine kinases in M. tuberculosis. Given the extensive knowledge base in kinase inhibition, these enzymes present an interesting opportunity for antimycobacterial drug discovery. This study focused on targeting both PknA and PknB while improving the selectivity window over related mammalian kinases. Compounds achieved potent inhibition (Ki ≈ 5 nM) of both PknA and PknB. A binding pocket unique to mycobacterial kinases was identified. Substitutions that filled this pocket resulted in a 100-fold differential against a broad selection of mammalian kinases. Reducing lipophilicity improved antimycobacterial activity with the most potent compounds achieving minimum inhibitory concentrations ranging from 3 to 5 μM (1-2 μg/mL) against the H37Ra isolate of M. tuberculosis.

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