Recombinant Human ARG1/Arginase-1 Protein, C-His from ProteoGenix; catalogue ARO-P10334; research use only.
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Recombinant proteins are proteins that are produced through genetic engineering techniques, where a specific gene of interest is inserted into a host organism, such as bacteria or yeast, to produce a large quantity of the desired protein. These proteins have become essential tools in various fields of research, including biotechnology, medicine, and diagnostics.
One such recombinant protein is Recombinant Human ARG1/Arginase-1 Protein, which has gained significant attention in recent years due to its unique structure, activity, and potential applications. In this article, we will delve deeper into the details of this protein and its role in various fields of science.
Recombinant Human ARG1/Arginase-1 Protein is a 354 amino acid protein with a molecular weight of approximately 40 kDa. It is a homotrimer, meaning it is composed of three identical subunits, each containing a catalytic domain and a zinc-binding domain. The protein is encoded by the ARG1 gene, located on chromosome 6 in humans.
The crystal structure of Recombinant Human ARG1/Arginase-1 Protein has been extensively studied, revealing its active site and the interactions between the subunits. The protein has a funnel-shaped active site, which binds to the substrate, arginine, and converts it into ornithine and urea. The zinc-binding domain plays a crucial role in stabilizing the active site and facilitating the catalytic reaction.
The main function of Recombinant Human ARG1/Arginase-1 Protein is to catalyze the hydrolysis of arginine, an essential amino acid, into ornithine and urea. This reaction is a crucial step in the urea cycle, which is responsible for removing excess nitrogen from the body. In addition to its role in the urea cycle, Recombinant Human ARG1/Arginase-1 Protein has been found to play a role in various other physiological processes, such as wound healing, immune response, and cell growth and differentiation.
The activity of Recombinant Human ARG1/Arginase-1 Protein has also been linked to several diseases, including cancer, cardiovascular diseases, and neurological disorders. In cancer, the overexpression of ARG1 has been observed in various types of tumors, leading to increased levels of ornithine, which promotes tumor growth and metastasis. In contrast, in cardiovascular diseases, the deficiency of ARG1 has been associated with impaired nitric oxide production, leading to endothelial dysfunction and hypertension.
Recombinant Human ARG1/Arginase-1 Protein has a wide range of potential applications in various fields of science. In biotechnology, it is used as a tool to study the role of arginine metabolism in different physiological processes. It is also used in the production of ornithine, which has various industrial applications, including the production of cosmetics and dietary supplements.
In medicine, Recombinant Human ARG1/Arginase-1 Protein has been investigated as a potential therapeutic agent for various diseases. Its ability to regulate arginine levels makes it a promising candidate for the treatment of arginine-related disorders, such as hyperargininemia. It has also been studied as a potential anti-cancer agent, with promising results in preclinical studies.
In diagnostics, Recombinant Human ARG1/Arginase-1 Protein has been used as a biomarker for various diseases, such as liver diseases and cancer. Its levels in blood and tissue samples can provide valuable information about the metabolic status of the body and the progression of certain diseases.
ProteoGenix catalogue number ARO-P10334. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 35.56 kDa; Fragment: Cys45-Lys322; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
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