Recombinant Human TAF13 protein

TAF13 (TATA-box binding protein associated factor 13) is a subunit of the TFIID complex, a critical general transcription factor required for RNA polymerase II-mediated gene transcription. As part of the TFIID complex, TAF13 plays a role in recognizing core promoter elements, facilitating the assembly of the pre-initiation complex, and regulating transcriptional initiation. Structurally, TAF13 contains conserved domains for protein-protein interactions, enabling its association with other TAFs (e.g., TAF11) and components of the transcriptional machinery.

Recombinant TAF13 protein is engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional TAF13 for biochemical and structural studies. Its recombinant form allows researchers to investigate TFIID assembly mechanisms, promoter-specific transcriptional regulation, and interactions with DNA or cofactors. For example, studies using recombinant TAF11/TAF13 heterodimers have revealed their role in stabilizing the TFIID architecture and mediating histone H3K4 methylation recognition.

TAF13 dysregulation has been implicated in diseases, including cancers and neurodevelopmental disorders, making its recombinant form valuable for drug discovery and mechanistic studies. Additionally, recombinant TAF13 enables the exploration of post-translational modifications (e.g., phosphorylation) that modulate transcriptional activity. Its use in *in vitro* assays (e.g., chromatin immunoprecipitation, pull-down experiments) has advanced our understanding of context-dependent transcriptional control and TFIID-related pathologies. Overall, recombinant TAF13 serves as a key tool for dissecting fundamental transcriptional processes and their disease linkages.