{"product_id":"cst-54268s","title":"CST,  54268S, TL12-186","description":"Chemical Modulators for studying in the research area.\n\n\u003cb\u003eProduct Usage Information\u003c\/b\u003e\nTL12-186 is supplied as a lyophilized powder. For a 5 mM stock, reconstitute 5 mg of powder in 1.07 mL of DMSO. Working concentrations and length of treatment can vary depending on the desired effect.\n\u003cb\u003eStorage\u003c\/b\u003e\nStore lyophilized at -20ºC, desiccated. In lyophilized form, the chemical is stable for 24 months. Once in solution, store at -20ºC and use within 3 months to prevent loss of potency. Aliquot to avoid multiple freeze\/thaw cycles .\n\u003cb\u003eBackground\u003c\/b\u003e\nTL12-186 is a pan-kinase PROTAC (proteolysis-targeting chimera) compound that links a cereblon (CRBN)-recruiting pomalidomide moiety and a promiscuous kinase inhibitor (1). The inhibitor moiety competes with ATP for binding to the kinase catalytic site. TL12-186 exhibits a binding affinity (IC ) of 12 nM for CRBN. At a concentration of 1 μM, TL12-186 induces \u0026gt;90% inhibition of 193 kinases according to a kinase selectivity assay. When administered at 100 nM for four hours in human MOLM-14 and MOLT-4 cells, TL12-186 degrades 28 kinases by 50% or more, including BTK, PTK2, PTK2B, FLT3, AURKA\/B, TEC, ULK1, ITK, and nine members of the CDK family. This compound is valuable for assessing the susceptibility of kinases to degradation in various model systems. In one study, a platelet model system treated with TL12-186 showed that BTK degradation has advantages over simple inhibition in preventing thrombosis (2). Additionally, TL12-186 was used to experimentally validate a computational model that predicts which substrate lysines are most likely to be ubiquitinated by CRBN-dependent PROTACs (3).","brand":"CST","offers":[{"title":"Default Title","offer_id":46800696148137,"sku":"54268S","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/products\/cst-54268s","provider":"Iright","version":"1.0","type":"link"}