99858-15-8 Usage
General Description
The chemical compound [(3,4-dichlorophenyl)methyl](2-methylpropyl)amine, also known as 2,2-dichloro-1-(3,4-dichlorophenyl)-3-methylbutylamine, is a combination of a dichlorophenylmethyl group and a 2-methylpropylamine group. It is commonly used in the production of pharmaceuticals and pesticides, due to its potential as an intermediate for the synthesis of various biologically active compounds. The compound is also used as a building block for the creation of new and novel molecules with potential applications in medicinal chemistry, agriculture, and other industries. Additionally, it exhibits potential anti-inflammatory and antitumor activities, making it a target for further research in drug development and disease treatment.
Check Digit Verification of cas no
The CAS Registry Mumber 99858-15-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,9,8,5 and 8 respectively; the second part has 2 digits, 1 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 99858-15:
(7*9)+(6*9)+(5*8)+(4*5)+(3*8)+(2*1)+(1*5)=208
208 % 10 = 8
So 99858-15-8 is a valid CAS Registry Number.
99858-15-8Relevant articles and documents
Novel non-ATP competitive small molecules targeting the CK2 α/β interface
Brear, Paul,North, Andrew,Iegre, Jessica,Hadje Georgiou, Kathy,Lubin, Alexandra,Carro, Laura,Green, William,Sore, Hannah F.,Hyv?nen, Marko,Spring, David R.
supporting information, p. 3016 - 3020 (2018/05/26)
Increased CK2 levels are prevalent in many cancers. Combined with the critical role CK2 plays in many cell-signaling pathways, this makes it a prime target for down regulation to fight tumour growth. Herein, we report a fragment-based approach to inhibiting the interaction between CK2α and CK2β at the α-β interface of the holoenzyme. A fragment, CAM187, with an IC50 of 44 μM and a molecular weight of only 257 gmol?1 has been identified as the most promising compound. Importantly, the lead fragment only bound at the interface and was not observed in the ATP binding site of the protein when co-crystallised with CK2α. The fragment-like molecules discovered in this study represent unique scaffolds to CK2 inhibition and leave room for further optimisation.
