Recombinant Human KAT5, N-His from ProteoGenix; catalogue ARO-P13196; research use only.
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Recombinant Human KAT5, also known as lysine acetyltransferase 5, is a protein that plays a crucial role in the regulation of gene expression through histone acetylation. It is a highly conserved protein found in all eukaryotic organisms and is involved in various biological processes such as cell growth, differentiation, and apoptosis. The recombinant form of this protein has been extensively studied and has shown promising results in various research fields, making it a valuable tool for scientists.
The recombinant form of Human KAT5 is a 604 amino acid protein with a molecular weight of approximately 68 kDa. It contains a conserved catalytic domain, known as the histone acetyltransferase (HAT) domain, which is responsible for its enzymatic activity. The HAT domain is located in the N-terminal region of the protein and is composed of a bromodomain, a PHD finger, and a C2HC zinc finger. These domains are important for the recognition and binding of histone substrates, as well as for the regulation of KAT5 activity.
In addition to the HAT domain, the recombinant Human KAT5 also contains a C-terminal domain, which is involved in protein-protein interactions. This domain is essential for the recruitment of KAT5 to specific gene loci and for its interaction with other transcriptional regulators. The overall structure of recombinant Human KAT5 is crucial for its function as a histone acetyltransferase and for its involvement in various cellular processes.
The primary function of recombinant Human KAT5 is to catalyze the transfer of an acetyl group from acetyl-CoA to lysine residues on histone proteins. This results in the neutralization of the positive charge on histones, leading to a more open chromatin structure and increased accessibility of DNA for transcriptional machinery. This process is crucial for the regulation of gene expression and is involved in various biological processes such as cell growth, differentiation, and apoptosis.
In addition to its role in histone acetylation, recombinant Human KAT5 has also been shown to acetylate non-histone proteins, such as p53 and E2F1, which are important regulators of cell cycle and apoptosis. This suggests that KAT5 may have additional functions beyond its role in chromatin remodeling. Furthermore, studies have shown that KAT5 is involved in DNA repair and maintenance of genomic stability, further highlighting its importance in cellular processes.
The recombinant form of Human KAT5 has a wide range of applications in scientific research. Its ability to acetylate histones and non-histone proteins makes it a valuable tool for studying gene expression, chromatin remodeling, and cellular processes. Recombinant Human KAT5 has been used in various studies to investigate its role in cancer, neurodegenerative diseases, and viral infections.
Furthermore, recombinant Human KAT5 has been used in drug discovery and development. Inhibition of KAT5 activity has been shown to have anti-cancer effects, making it a potential target for cancer therapy. Additionally, studies have shown that KAT5 inhibitors can also have anti-inflammatory effects, making it a potential target for the treatment of inflammatory diseases.
In conclusion, recombinant Human KAT5 is a highly conserved protein with a crucial role in the regulation of gene expression. Its structure, activity, and various applications make it a valuable tool for scientific research. Further studies on KAT5 and its interactions with other proteins may provide a deeper understanding of its functions and potential therapeutic applications.
ProteoGenix catalogue number ARO-P13196. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 42.63 kDa; Fragment: Ala101-Ser457; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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