TRIM24 Protein, Human (P. pastoris, His)

TRIM24 protein is a multifunctional coactivator that dynamically interacts with nuclear receptors and coactivators to influence target gene transcription. It binds preferentially to unmodified H3K4me0 and acetylated H3K23. TRIM24 Protein, Human (P. pastoris, His) is the recombinant human-derived TRIM24 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of TRIM24 Protein, Human (P. pastoris, His) is 122 a.a., with molecular weight of 16.5 kDa.

TRIM24, a versatile transcriptional coactivator, dynamically interacts with numerous nuclear receptors and coactivators, influencing the transcriptional landscape of target genes. Its binding to chromatin is notably influenced by histone H3 modifications, showing a preference for histone H3 that is unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Beyond its coactivator role, TRIM24 exhibits E3 protein-ubiquitin ligase activity. In the DNA damage response, a regulatory interplay unfolds wherein ATM kinase phosphorylates TRIM24 early in the response, leading to its ubiquitination and degradation. Upon sufficient DNA repair, TP53 activates TRIM24 transcription, initiating a feedback loop that results in TRIM24-mediated TP53 ubiquitination and degradation. This dual regulatory mechanism underscores TRIM24's pivotal role in the delicate balance between cell proliferation and apoptosis. Furthermore, TRIM24 extends its influence to innate immunity by orchestrating the 'Lys-63'-linked ubiquitination of TRAF3, activating downstream signaling in the type I IFN pathway. Notably, TRIM24 also exerts a negative regulatory effect on NLRP3/CASP1/IL-1beta-mediated pyroptosis and cell migration, possibly through the ubiquitination of NLRP3.

Human

P. pastoris

N-6*His

O15164 (K891-K1012)

8805  [NCBI]

KKKTEGLVKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYSMYSKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLENYFEELLKNLYPEKRFPK

16.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.