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RKS262

(CAS: 1041469-97-9)

Suppliers of RKS262

Company Name Email Tel Country
BOC Sciences [email protected] 1-631-504-6093

Fax: 1-631-614-7828Purity: Brand: BOC Sciences

MedKoo Biosciences, Inc. [email protected] 919-279-0682 USA

Fax: 919-980-4831Purity: Brand:

Shanghai Haoyuan Chemexpress Co., Ltd. [email protected] +86 (21) 5187-0955 / +86 (21) 5895-5995 China

Fax: +86 (21) 5895-5996Purity: Brand:

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Background Information of RKS262

RKS262 is a CDK1/4  inhibitor.

Solubility of RKS262

Solubility Sources

Storage Condition of RKS262

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MSDS Information

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Quality Control and Spectral Data

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Mechanism and Indications

Signaling Pathways Cell Cycle/DNA Damage
Target CDK
Research Area Cancer
Indications

Clinical Information

Product Name Sponsor & Collaborators Indications Start Date End Date Phase

Chemical Information

M.Wt Formula CAS No. Synonyms
433.7 C15H14BrClN2O4S 1041469-97-9 RKS262; RKS 262; RKS-262

Structure Information of RKS262

Smiles C1(=O)OC2=CC=C(Br)C=C2C(Cl)=C1/C=N/N1CCS(=O)(=O)CC1C
InChI InChI=1S/C15H14BrClN2O4S/c1-9-8-24(21,22)5-4-19(9)18-7-12-14(17)11-6-10(16)2-3-13(11)23-15(12)20/h2-3,6-7,9H,4-5,8H2,1H3/b18-7+

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Chemical and Physical Properties

Appearance: Melting point:
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Water Solubility: Solubility:Soluble in DMSO
Density: Merck:
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Vapour: EINECS:
Optical Rotation: alpha:

Reference

[1].Tutone M, et al. Recent advances on CDK inhibitors: An insight by means of in silico methods. Eur J Med Chem. 2017 Dec 15;142:300-315.
The cyclin dependent kinases (CDKs) are a small family of serine/threonine protein kinases that can act as a potential therapeutic target in several proliferative diseases, including cancer. This short review is a survey on the more recent research progresses in the field achieved by using in silico methods. All the "armamentarium" available to the medicinal chemists (docking protocols and molecular dynamics, fragment-based, de novo design, virtual screening, and QSAR) has been employed to the discovery of new, potent, and selective inhibitors of cyclin dependent kinases. The results cited herein can be useful to understand the nature of the inhibitor-target interactions, and furnish an insight on the structural/molecular requirements necessary to achieve the required selectivity against cyclin dependent kinases over other types of kinases.

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