TAF9 Human
Description
TAF9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
TAF9 is a multisubunit complex that includes a small TATA-binding polypeptide and other TBP-associated factors (TAFs). The recombinant human TAF9 protein is typically produced in Escherichia coli (E. coli) and is fused to a His-tag at the N-terminus to aid in purification. The protein consists of 192 amino acids, with a molecular mass of approximately 22.2 kDa .
The primary function of TAF9 is to facilitate the assembly of the preinitiation complex through direct interactions with the TATA promoter element. This interaction is crucial for the accurate initiation of transcription, ensuring that genes are expressed at the right time and in the right amounts.
Recombinant human TAF9 protein is produced using conventional chromatography techniques. The protein is expressed in E. coli and purified to a high degree of purity, typically greater than 90% as determined by SDS-PAGE . The His-tag at the N-terminus allows for easy purification using nickel affinity chromatography, which binds to the histidine residues in the tag.
TAF9 recombinant protein is primarily used in research settings to study the mechanisms of transcription initiation and the role of TAFs in gene expression. It is also used in various biochemical assays to investigate protein-protein interactions and the assembly of the preinitiation complex.
For optimal stability, TAF9 recombinant protein should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain the protein’s integrity. The protein is typically supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 1 mM DTT, with no added preservatives .
