Mz1, selectively degrades BRD4
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(1 Publication)
MW 1002.6 Da, Purity >98%. Cell penetrant PROTAC (Proteolysis Targeting Chimera) compound based on (+)-JQ1 (ab141498) tethered to a von Hippel-Lindau (VHL) ligand. Retains high affinity for BRD2, BRD3 and BRD4 bromodomains. Induces preferential degradation of BRD4 over BRD2 and BRD3 in HeLa cells.
View Alternative Names
2610203G15Rik, 2900045O07Rik, AF229032, AW108261, BRD4-NUT FUSION, BRD4-NUT fusion oncoprotein, BRD4_HUMAN, Bromodomain containing 4, Bromodomain-containing protein 4, CAP, CRBN_HUMAN, Cereblon, DDB p127 subunit, DDB1_HUMAN, DDBa, DKFZp781K0715, DNA damage-binding protein 1, DNA damage-binding protein a, Damage-specific DNA-binding protein 1, ELOB_HUMAN, ELOC_HUMAN, Elongin 15 kDa subunit, Elongin 18 kDa subunit, Elongin binding protein, Elongin-B, Elongin-C, G7 protein, HBV X-associated protein 1, HRCA 1, HUNK1, HUNKI, MCAP, MGC27358, MRT2A, Mitotic chromosome-associated protein, OTTHUMP00000209555, Protein G7, Protein HUNK1, Protein cereblon, Protein x 0001, RCA 1, RNA polymerase II transcription factor SIII p18 subunit, RNA polymerase II transcription factor SIII subunit B, RNA polymerase II transcription factor SIII subunit C, SIII, SIII p15, SIII p18, TCEB 1, TCEB 2, Transcription elongation factor B (SIII) polypeptide 1, Transcription elongation factor B (SIII) polypeptide 2, Transcription elongation factor B polypeptide 1, Transcription elongation factor B polypeptide 2, UV-DDB 1, UV-damaged DNA-binding factor, UV-damaged DNA-binding protein 1, VHL 1, VHLH, VHL_HUMAN, Von Hippel Lindau, Von Hippel Lindau tumor suppressor, E3 ubiquitin protein ligase, Von Hippel-Lindau disease tumor suppressor, X associated protein 1, XAP-1, XPCe, XPE, XPE-BF, XPE-binding factor, Xeroderma pigmentosum group E-complementing protein, chromosome associated protein, pVHL, piL, von Hippel Lindau syndrome, von Hippel Lindau tumor suppressor
- Chemical Structure
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Chemical Structure - Mz1, selectively degrades BRD4 (AB230371)
2D chemical structure image of ab230371, Mz1, selectively degrades BRD4
Properties and storage information
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
DDB1 Von Hippel Lindau BRD4 and CRBN participate in important cellular processes such as transcriptional regulation and protein degradation. BRD4 when bound to acetylated lysines on histones helps regulate gene expression by recruiting transcriptional machinery to target genes. MZ1 and JQ1 specific small-molecule inhibitors modulate BRD4 function. In various complexes like the Elongin BC complex Elongin B and C stabilize these functions participating in elongation and transcription regulation processes. CRBN modulates the function of specific target proteins by promoting their ubiquitination and subsequent proteasomal degradation.
Pathways
These proteins integrate into the ubiquitin-proteasome system and transcriptional regulatory pathways. DDB1 collaborates with CUL4A in DNA damage repair and cell cycle control. VHL associates within the hypoxia signaling pathway by mediating the degradation of HIF1α under normoxic conditions. This degradation prevents uncontrolled cell growth and angiogenesis. On the other hand BRD4 takes part in the transcription elongation process and interacts with MZ-1 a potent PROTAC that alters chromatin structure to influence gene expression.
Publications (1)
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Cell death & disease 13:921 PubMed36333293
2022
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