Recombinant Human ATAD2 Protein, N-His

Reference: YHJ07602
Product nameRecombinant Human ATAD2 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight34.94 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 TypeSer432-Arg722
Aliases /SynonymsAAA nuclear coregulator cancer-associated protein, ANCCA, ATAD2, ATPase family AAA domain-containing protein 2
ReferenceYHJ07602
NoteFor research use only.

Description of Recombinant Human ATAD2 Protein, N-His

Introduction

Recombinant Human ATAD2 Protein, also known as ATPase family AAA domain-containing protein 2, is a protein that plays a crucial role in chromatin remodeling and transcriptional regulation. It is encoded by the ATAD2 gene and is found in humans, with a molecular weight of approximately 170 kDa.

Structure of Recombinant Human ATAD2 Protein

Recombinant Human ATAD2 Protein is composed of 1506 amino acids and contains several functional domains, including an AAA ATPase domain, a bromodomain, and a helicase domain. The AAA ATPase domain is responsible for the ATPase activity of the protein, while the bromodomain is involved in recognizing and binding to acetylated lysine residues on histones. The helicase domain allows the protein to unwind DNA, facilitating transcriptional regulation.

Activity of Recombinant Human ATAD2 Protein

Recombinant Human ATAD2 Protein is a key player in chromatin remodeling, a process that regulates gene expression by altering the accessibility of DNA to transcription factors. It does so by binding to acetylated histones and recruiting other chromatin remodeling proteins, such as histone acetyltransferases and deacetylases. This leads to changes in the structure of chromatin, making certain regions of DNA more or less accessible for transcription.

In addition to its role in chromatin remodeling, Recombinant Human ATAD2 Protein also has ATPase and helicase activities. These activities are essential for the protein’s function in DNA replication and repair, as well as in transcriptional regulation. By unwinding DNA and hydrolyzing ATP, the protein can facilitate the binding of transcription factors to specific regions of DNA, thus regulating gene expression.

Application of Recombinant Human ATAD2 Protein

Recombinant Human ATAD2 Protein has been studied extensively for its role in cancer development and progression. It has been found to be overexpressed in various types of cancer, including breast, lung, and ovarian cancer. This overexpression has been linked to increased cell proliferation, migration, and invasion, making Recombinant Human ATAD2 Protein a potential therapeutic target for cancer treatment.

Additionally, studies have shown that Recombinant Human ATAD2 Protein is involved in the development of drug resistance in cancer cells. It has been found to interact with other proteins involved in drug resistance, such as P-glycoprotein and multidrug resistance-associated protein 1, and contribute to their overexpression. This highlights the potential of Recombinant Human ATAD2 Protein as a biomarker for predicting drug resistance and as a target for overcoming it.

Furthermore, Recombinant Human ATAD2 Protein has been implicated in other diseases, such as neurodegenerative disorders and viral infections. It has been found to interact with proteins involved in the replication of viruses, such as hepatitis C virus and human papillomavirus, suggesting a potential role in viral pathogenesis.

Conclusion

In summary, Recombinant Human ATAD2 Protein is a multifunctional protein with crucial roles in chromatin remodeling and transcriptional regulation. Its structure, activity, and application have been extensively studied, particularly in the context of cancer development and drug resistance. Further research on this protein may lead to a better understanding of its role in various diseases and the development of targeted therapies.

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