Recombinant Human TAF1 Protein, N-His

Reference: YHD46801
Product nameRecombinant Human TAF1 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight38.30 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeSer635-Gly944
Aliases /Synonymsp250, TAF(II)250, CCGS, BA2R, TAF1, Transcription initiation factor TFIID subunit 1, Cell cycle gene 1 protein, TAFII-250, TAF2A, CCG1, TBP-associated factor 250 kDa, Transcription initiation factor TFIID 250 kDa subunit, TAFII250
ReferenceYHD46801
NoteFor research use only.

Description of Recombinant Human TAF1 Protein, N-His

Introduction

Recombinant Human TAF1 Protein, also known as TATA-binding protein-associated factor 1, is a crucial component of the general transcription factor complex TFIID. It plays a key role in the initiation of transcription by binding to the TATA box, a DNA sequence found in the promoter regions of most eukaryotic genes. This protein is encoded by the TAF1 gene located on chromosome X and is highly conserved in different species, including humans.

Structure of Recombinant Human TAF1 Protein

Recombinant Human TAF1 Protein is a large protein with a molecular weight of approximately 250 kDa. It consists of 14 conserved domains, including a TATA box-binding domain, a histone fold domain, and multiple glutamine-rich domains. These domains are responsible for its various functions, such as DNA binding, protein-protein interactions, and transcriptional activation.

The crystal structure of Recombinant Human TAF1 Protein has been determined, revealing its three-dimensional organization. It forms a saddle-shaped structure with a central cavity, which accommodates the TATA box DNA. This structure is essential for the specific recognition and binding of the TATA box, thereby initiating the transcription process.

Activity of Recombinant Human TAF1 Protein

Recombinant Human TAF1 Protein is a key player in the assembly of the pre-initiation complex (PIC) at the promoter region of genes. It interacts with other components of the general transcription factor complex TFIID, including TBP (TATA-binding protein) and TAFs (TBP-associated factors), to form the functional PIC. This complex then recruits RNA polymerase II to the promoter, leading to the initiation of transcription.

Moreover, Recombinant Human TAF1 Protein has been shown to have a role in chromatin remodeling and gene regulation. It can interact with histone acetyltransferases and histone deacetylases, which modify the histone proteins associated with DNA. This interaction results in the relaxation or tightening of the chromatin structure, allowing or preventing the access of transcription factors to the DNA, respectively.

Application of Recombinant Human TAF1 Protein

Recombinant Human TAF1 Protein has been widely used in various research studies and applications. It is commonly used as an antigen in the production of antibodies for studying its structure and function. These antibodies can also be used for immunoprecipitation and chromatin immunoprecipitation assays to study its binding partners and gene regulation.

Furthermore, Recombinant Human TAF1 Protein has been utilized in drug discovery and development. Its role in transcriptional activation makes it a potential target for therapeutic interventions in diseases where gene expression is dysregulated. In addition, its interaction with histone-modifying enzymes makes it a valuable tool for studying epigenetic mechanisms and their role in diseases such as cancer.

In conclusion, Recombinant Human TAF1 Protein is a crucial component of the transcription machinery, involved in the initiation of transcription and gene regulation. Its structure and function have been extensively studied, and it has various applications in research and drug development. Further studies on this protein may provide valuable insights into its role in diseases and potential therapeutic targets.

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