Recombinant Human MACROH2A2 Protein, N-His from ProteoGenix; catalogue ARO-P11696; research use only.
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Recombinant proteins have revolutionized the field of biotechnology and have become essential tools in various scientific and medical applications. One such protein is the Recombinant Human MACROH2A2 Protein, which has gained significant attention in recent years due to its unique structure, diverse activities, and potential therapeutic applications. In this article, we will explore the structure, activity, and application of this recombinant protein in detail.
The Recombinant Human MACROH2A2 Protein, also known as macroH2A.2, is a member of the macroH2A family of histone variants. It is encoded by the MACROH2A2 gene located on chromosome 20q13.33 in humans. The protein consists of 383 amino acids with a molecular weight of approximately 40 kDa. It contains a central globular domain, a highly conserved C-terminal histone fold domain, and a variable N-terminal tail region.
The most striking feature of the MACROH2A2 protein is its unique C-terminal histone fold domain, which has an extended structure compared to other histone variants. This domain contains a highly conserved macro domain, which is involved in various cellular processes such as DNA repair, transcription, and chromatin remodeling. The N-terminal tail region of the protein is rich in lysine residues, which are potential sites for post-translational modifications, including acetylation, methylation, and phosphorylation.
The Recombinant Human MACROH2A2 Protein has diverse activities that are crucial for maintaining genomic stability and regulating gene expression. It has been reported to play a role in DNA damage response by facilitating the recruitment of repair proteins to the damaged sites. Additionally, it is involved in transcriptional regulation by modulating the accessibility of DNA to transcription factors and RNA polymerase.
The macroH2A.2 protein has also been linked to cellular senescence, a process that limits the proliferative capacity of cells and plays a critical role in aging and age-related diseases. Studies have shown that the overexpression of this protein can induce senescence in cancer cells, making it a potential target for cancer therapy.
The unique structure and diverse activities of the Recombinant Human MACROH2A2 Protein make it a valuable tool in various scientific and medical applications. One of its primary applications is in the study of epigenetics, a field that investigates heritable changes in gene expression without altering the DNA sequence. The macroH2A.2 protein is an essential epigenetic regulator, and its recombinant form is widely used in research to understand its role in chromatin remodeling and gene expression.
Furthermore, the MACROH2A2 protein has potential therapeutic applications in cancer treatment. As mentioned earlier, its overexpression can induce cellular senescence in cancer cells, making it a promising target for cancer therapy. Additionally, studies have shown that the protein is downregulated in various cancers, and its restoration can inhibit tumor growth and metastasis.
In conclusion, the Recombinant Human MACROH2A2 Protein is a unique and versatile protein with diverse activities and potential therapeutic applications. Its recombinant form has become an essential tool in various fields, including epigenetics and cancer research. Further studies on this protein may reveal new insights into its functions and potential applications in the future.
ProteoGenix catalogue number ARO-P11696. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 22.98 kDa; Fragment: Gly182-Lys372; 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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Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
