Lipids & Polymers

PROTAC BET Degrader-1 is a bifunctional molecule that links Cereblon and BET ligands, effectively reducing the levels of BRD2, BRD3, and BRD4 proteins. Its functional groups enable targeted protein degradation at low concentrations

PROTAC BRD4 Degrader-1 is a bifunctional molecule linking Cereblon and BRD4 ligands, designed to target and degrade BRD4 protein. Its structure enables effective reduction of BRD4 levels and modulation of c-Myc expression.

PROTAC ERα Degrader-1 is a molecule consisting of an E3 ligase ligand, a linker, and an estrogen receptor-alpha (ERα) targeting group, facilitating targeted degradation of ERα.

HDAC6 Degrader-1 is a PROTAC that utilizes Nexturastat A as a selective HDAC6-binding component, combined with a linker and an E3 ligase-recruiting ligand. This structure promotes targeted degradation of HDAC6, offering strong selectivity over other HDAC enzymes and effectively inhibiting cell proliferation.

MI-389 is a PROTAC designed to degrade the translation termination factor GSPT1. It disrupts a critical target shared across various AML and ALL cell lines, with its activity dependent on CRL4 CRBN E3 ligase recruitment.

KTX-582 is a potent PROTAC targeting the degradation of IRAK4 and Ikaros. It promotes apoptosis in MYD88 mutant cell lines and demonstrates efficacy in inducing tumor regression in lymphoma models.

YD23 is a PROTAC molecule designed to target and degrade SMARCA2, exploiting the synthetic lethality with SMARCA4. It modulates chromatin accessibility, particularly at gene enhancers involved in cell cycle and growth regulation, with selective effects in SMARCA4-deficient cells.

MS4322 isomer is an isomer of a selective PRMT5 degrader, designed to target and degrade protein arginine methyltransferase 5. Its activity includes inhibiting the growth of various cell lines, highlighting its role in modulating PRMT5-related processes.

PROTAC IDO1 Degrader-1 is a bifunctional molecule designed to target indoleamine 2,3-dioxygenase 1 (IDO1) for degradation by recruiting it to the Cereblon E3 ligase, leading to its ubiquitination and subsequent breakdown via the ubiquitin-proteasome system. It has been shown to enhance the activity of certain immune cells in a research context.