Anti-TATA Binding Protein [Clone 1TBP18] - 200 μg

The TATA-binding protein (TBP) plays a central role in the assembly of most eukaryotic transcription initiation complexes. TBP assembles with other proteins to form unique multimeric complexes for each of the three different nuclear RNA polymerases. TBP has been cloned from a variety of species and consists of two distinct domains. The C-terminal domain (~180 amino acids) is highly conserved among species, whereas the N-terminal domain varies considerably in length and sequence among different species. The conserved C-terminal domain contains the DNA-binding region as well as regions that interact with positive and negative regulatory proteins. In human TBP, the non-conserved N-terminal domain includes a stretch of glutamine residues ranging from 26 to 42. Several research groups have found an association between expansion of this polyglutamine tract with rare forms of spinocerebellar ataxia and other neurodegenerative diseases including Huntington's disease. Key Features and Scientific Rationale of Anti-TBP (Clone 1TBP18) : Ubiquitous Transcriptional Core Factor: TBP is the foundational subunit of Transcription Factor II D (TFIID) and is indispensable for the accurate initiation of transcription by all three nuclear RNA polymerases (Pol I, Pol II, and Pol III) . Its precise binding to the TATA box sequence within promoter regions dictates the assembly of the pre-initiation complex. Our antibody provides a robust means to investigate this central orchestrator of eukaryotic gene expression and transcriptional regulation. Critical Reagent for Polyglutamine Disease Research: The N-terminal domain of human TBP contains a polymorphic polyglutamine (polyQ) tract (26-42 residues) . Pathological expansions of this glutamine repeat are directly implicated in the etiology of several debilitating neurodegenerative diseases, including Huntington's disease and specific forms of spinocerebellar ataxia (SCA17) . Our Anti-TBP antibody (Clone 1TBP18) is an invaluable tool for: Probing the cellular localization and expression levels of TBP in disease models. Investigating the impact of polyQ expansions on TBP function and protein aggregation. Exploring the molecular pathology and potential therapeutic strategies for polyglutamine disorders.