KDT-11|CAS |DC Chemicals

Cas No.:
Chemical Name:	KDT-11
Formula:	C₆₆H₈₉ClFN₇O₉
M.Wt:	1178.93

Cat. No.	Product name	Field of application
DC29221	PTP1B-IN-9	PTP1B-IN-9 is a ubiquitin-proteasome system (UPS)-stressor. PTP1B-IN-9 inhibits ubiquitin-mediated protein degradation upstream of the 20S proteasomal catalytic activites. PTP1B-IN-9 triggers a ubiquitin-proteasome-system (UPS)-stress response without affecting 20S proteasome catalytic activities. Anticancer activity.
DC11125	TCH-165	TCH-165 is a specific small molecule modulator of proteasome assembly, regulates the dynamic equilibrium between the 20S and 26S proteasome complexes, favoring 20S-mediated protein degradation.
DC10304	RA190	RA190, a bis-benzylidine piperidon, inhibits proteasome function by covalently binding to cysteine 88 of ubiquitin receptor RPN13.
DC4243	ONX-0914	ONX 0914 is an immunoproteasome inhibitor with potential treatment applications in autoimmune disorders, such as rheumatoid arthritis, inflammatory bowel disease and lupus.
DC5086	Ixazomib(MLN2238)	MLN2238 inhibits the chymotrypsin-like proteolytic (β5) site of the 20S proteasome with IC50 and Ki of 3.4 nM and 0.93 nM, respectively, also inhibits the caspase-like (β1) and trypsin-like (β2) proteolytic sites, with IC50 of 31 and 3500 nM.
DC77117	Boc3Arg	Boc3Arg is the tert-butyl carbamate-protected arginine. Boc3Arg is an efficient tag to induce degradation through directly localizing the protein to the 20S proteasome.
DC74328	WZ-1831	WZ-1831 is a potent and highly selective inhibitor of human constitutive proteasome chymotryptic activity (β5c) with IC50 of 10 nM, >500-fold selectivity over β5i (IC50=7.1 uM).
DC74327	TXS-8	TXS-8 is a specific, small molecule binder of Rpn-6 with KD of 14 uM, Rpn-6 is a subunit of the 19S regulatory particle (RP) of 26s proteasome.
DC74326	TCL-Ester	TCL-Ester is the cell-permeable derivative of TCL-1, a non-covalent ligand targeting the Pru domain of Rpn-13.
DC74325	TCL-1	TCL-1 is a non-covalent ligand targeting the Pru domain of Rpn-13, TCL-1 binds to the Pru domain at the Rpn-2 docking site, affects proteasome-mediated proteolysis.