Recombinant Human PHPT1, N-His from ProteoGenix; catalogue ARO-P13063; research use only.
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Recombinant Human PHPT1 is a protein that plays an important role in cellular metabolism and has been extensively studied for its potential therapeutic applications. This protein is encoded by the PHPT1 gene and is a member of the phosphohistidine phosphatase family. It is composed of 149 amino acids and has a molecular weight of approximately 17 kilodaltons. The structure of Recombinant Human PHPT1 has been determined through X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, revealing a highly conserved active site and a unique catalytic mechanism.
The active site of Recombinant Human PHPT1 is located in a cleft between two domains, the N-terminal and C-terminal domains. This cleft contains a highly conserved catalytic triad consisting of a cysteine residue, a histidine residue, and an aspartate residue. The cysteine residue acts as a nucleophile, attacking the phosphate group of the substrate, while the histidine residue acts as a general acid/base, facilitating the transfer of a proton during the catalytic reaction. The aspartate residue helps to stabilize the transition state of the reaction.
The catalytic mechanism of Recombinant Human PHPT1 involves the dephosphorylation of phosphohistidine residues in proteins. Phosphohistidine is a rare post-translational modification that plays a crucial role in cellular signaling and regulation. Recombinant Human PHPT1 specifically targets phosphohistidine residues and removes the phosphate group, converting them back to histidine residues. This dephosphorylation reaction is essential for maintaining proper cellular function and has been linked to various diseases, making Recombinant Human PHPT1 a potential therapeutic target.
Recombinant Human PHPT1 is involved in several metabolic pathways, including the regulation of glucose and lipid metabolism. It has been shown to play a role in insulin signaling, as well as in the breakdown of fatty acids. Additionally, Recombinant Human PHPT1 has been linked to the regulation of cell growth and proliferation, making it a potential target for cancer treatment.
Recombinant Human PHPT1 has been extensively studied for its potential therapeutic applications. Due to its role in cellular metabolism and its involvement in various diseases, it has been identified as a potential target for drug development. Recombinant Human PHPT1 inhibitors have been developed and tested for their ability to treat diseases such as diabetes, obesity, and cancer. Additionally, Recombinant Human PHPT1 has been used as a tool in research to study the role of phosphohistidine in cellular signaling and regulation.
Recombinant Human PHPT1 is produced through genetic engineering techniques, where the PHPT1 gene is inserted into a host organism, such as bacteria or yeast. The host organism then produces the Recombinant Human PHPT1 protein, which can be purified and used for various applications. This recombinant protein is highly pure and has been extensively characterized to ensure its quality and activity.
In summary, Recombinant Human PHPT1 is a protein with a highly conserved structure and a unique catalytic mechanism. It plays a crucial role in cellular metabolism and has been identified as a potential therapeutic target for various diseases. Its production through genetic engineering techniques has allowed for the development of Recombinant Human PHPT1 inhibitors and its use as a tool in research. Further studies on this protein will continue to shed light on its role in cellular function and its potential as a therapeutic agent.
ProteoGenix catalogue number ARO-P13063. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 16.14 kDa; Fragment: Met1-Tyr125; Buffer: Lyophilized from a solution in PBS pH 7.4, 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.
