I-CBP112

Antagonizes interaction with acetylated lysine of EP300, CREBBP

Structure

Information

Protein target names: EP300 CREBBP

Mechanism of action: Antagonizes interaction with acetylated lysine

In Vitro Validations

Uniprot ID: Q09472
Target Class: Epigenetic
Target SubClass: Bromodomain
Potency: Kd
Potency Value: 167 nM
Potency Assay: ITC
PDB ID for probe-target interaction (3D structure): --
Target aliases:
Histone acetyltransferase p300, P300, EP300, EP300 ...

DOI Reference: 10.1158/0008-5472.CAN-15-0236

In Cell Validations

In Vivo Data

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SERP ratings and comments


SERP Ratings

In Cell Rating
In Model Organisms

(last updated: 20 Jan 2017 )

SERP Ratings

In Cell Rating
In Model Organisms

Comments:

I-CBP112 is a ligand of the highly conserved bromodomain of both CBP and p300. In vitro, the probe displays selective binding to CBP/p300 bromodomains with a Kd ~600 nM. Comparatively, the Kd for the bromodomains of BRD4 are ~5 and ~20 micromolar, so some off-target effects may be observed at higher concentrations in cells. Notably, I-CBP112 does not seem to displace CBP/p300 from acetylated chromatin, so cellular effects may be through as-of-yet undetermined mechanisms, perhaps through allosteric modulation (PMID:27332697). No pharmacokinetic data in animals has been published for this probe at this time, so its utility in model organisms remains to determined.

(last updated: 31 Mar 2017 )

SERP Ratings

In Cell Rating
In Model Organisms

Comments:

Bromodomain probe with selectivity for CBP/p300 outside of the BET family. This probe is able to displace p300 and CBP from acetylated proteins at low micromolar concentrations. Use at concentrations 1,000 - 5,000 nM appropriate in cellular assays. At concentrations higher than this range, 'off targeting' of BRD4 may be observed.

(last updated: 6 Apr 2017 )