Recombinant Human Arginase, Liver

• Cat.No.: ARG1-594H
• Product Overview: Recombinant full length human arginase I protein produced inE. coli.

Specification

• Cat. No.: ARG1-594H
• Description: Arginase is the fifth and final step in the urea cycle, a series of biophysical reactions in mammals during which the body disposes of harmful ammonia. Specifically, arginase converts L-arginine into L-ornithine and urea.[1] In most mammals, two isozymes of this enzyme exist; the first, Arginase I, functions in the urea cycle, and is located primarily in the cytoplasm of the liver.
• Source: E. coli.
• Purity: ≥90% (SDS-PAGE).
• Formulation: Liquid. In 10mM TRIS-HCl, pH 7.5, containing 1mM β-mercaptoethanol, 1mM MnCl2 and 50% glycerol.
• Specific Activity: ±2.0U/µg protein. One unit is defined as the amount of enzyme that converts 1µmol of L-arginine to L-ornithine and urea per min. at 37°C, pH 9.5 (R.T. Schminke, et al.; J. Biol. Chem. 238, 1012 (1962)).
• Storage: -80°C.
• Pathways: Arginine and proline metabolism; Metabolic pathways; Metabolism of amino acids and derivatives
• Tag: Non

Gene Information

• Gene Name: ARG1 arginase, liver [ Homo sapiens ]
• Synonyms: arginase, liver; ARG1; arginase-1; arginase 1; type I arginase; liver-type arginase; EC 3.5.3.1; Type I arginase; Liver-type arginase
• Gene ID: 383
• mRNA Refseq: NM_000045
• Protein Refseq: NP_000036
• MIM: 608313
• UniProt ID: P05089
• Chromosome Location: 6q23
• Function: arginase activity; hydrolase activity; metal ion binding

Reviews

03/21/2023

They may offer educational resources such as technical guides, protocols, and application notes, which can aid researchers in understanding the principles, techniques, and potential applications of ARG1 protein in their studies.

09/25/2022

Whether it be troubleshooting issues, offering experimental guidance, or addressing any concerns, the manufacturer's technical support ensures that researchers have a reliable and knowledgeable resource to rely on.

05/25/2022

These resources can enhance the efficiency and accuracy of experimental workflows and contribute to successful outcomes.

07/17/2021

Their collaboration, expertise, and customized solutions contribute to the successful execution of experiments, reliable data generation, and the advancement of scientific knowledge in the field.

06/04/2021

the manufacturer understands the importance of customization and can offer tailored solutions to meet specific research needs.

03/17/2021

the manufacturer's support is crucial for researchers using ARG1 protein in trials.

09/12/2020

In addition to its scientific merits, the manufacturer of ARG1 protein stands out for its outstanding technical support.

11/07/2018

The company provides a dedicated team of experts who are readily available to assist researchers throughout their experimental journey.

Q&As

Is there any link between ARG1 and metabolic disorders?

Yes, there is evidence linking ARG1 to metabolic disorders. Argininemia, a disorder caused by ARG1 deficiency, is characterized by disturbances in arginine metabolism. Additionally, dysregulated ARG1 activity has been observed in conditions such as obesity, insulin resistance, and non-alcoholic fatty liver disease (NAFLD). ARG1-mediated alterations in arginine metabolism can impact nitric oxide production, urea cycle function, and other pathways involved in metabolic regulation.

Are there any natural substances or dietary factors that can affect ARG1 activity?

Yes, certain natural substances and dietary factors have been shown to modulate ARG1 activity. For instance, polyphenols found in fruits and vegetables, such as quercetin and resveratrol, have been reported to inhibit ARG1 activity. Additionally, omega-3 fatty acids, present in fish oils, have been found to reduce ARG1 expression and activity in certain tissues.

Is there any relationship between the ARG1 protein and brain health or neurological disorders?

Although the primary role of ARG1 is in arginine metabolism and urea production, studies have suggested potential links between ARG1 and brain health. For example, alterations in the arginine-ornithine-urea pathway have been observed in disorders like Alzheimer's disease, suggesting a possible involvement of ARG1. However, the mechanisms and implications of ARG1 in brain function and neurological disorders are still being explored.

Are there any known mutations in the ARG1 gene associated with human diseases?

Yes, mutations in the ARG1 gene can lead to a rare genetic disorder called argininemia. Argininemia is an autosomal recessive disorder characterized by the accumulation of arginine in the blood and tissues due to a deficiency of ARG1 activity. It can cause symptoms such as developmental delay, intellectual disability, seizures, and progressive neurological deterioration.

Is ARG1 associated with any other physiological processes or diseases?

ARG1 has been implicated in various physiological processes beyond arginine metabolism and the urea cycle. It is involved in wound healing and tissue repair, where it promotes collagen production and fibroblast proliferation. Additionally, ARG1 has been linked to conditions such as asthma and chronic obstructive pulmonary disease (COPD), where increased ARG1 activity in the lungs may contribute to airway constriction and respiratory symptoms.

Are there any diseases associated with abnormal ARG1 activity?

Yes, there are diseases associated with abnormal ARG1 activity. Argininemia is a rare genetic disorder characterized by a deficiency of ARG1 activity, leading to the accumulation of arginine in the blood and tissues. This can cause neurological impairments, developmental delays, and other symptoms. Additionally, altered ARG1 expression or activity has been implicated in conditions such as asthma, allergic inflammation, and certain types of cancer.

Can the function of the ARG1 protein be inhibited or blocked?

Yes, the function of ARG1 can be inhibited or blocked using specific inhibitors. Some compounds, such as Nω-hydroxy-L-arginine (NOHA) and S-(2-boronoethyl)-L-cysteine (BEC), have been found to selectively inhibit ARG1 activity. These inhibitors can be useful in studying the biological role of ARG1 and developing potential therapeutic strategies.

Can variations in the ARG1 gene affect its activity or function?

Yes, genetic variations or mutations in the ARG1 gene can alter its activity or function. In argininemia, for instance, mutations in the ARG1 gene lead to reduced or absent ARG1 activity, resulting in the accumulation of arginine. Similarly, other genetic variations may affect ARG1 expression levels, enzymatic activity, or stability, potentially influencing its role in various physiological processes and disease conditions.

Can ARG1 activity be targeted for therapeutic interventions?

Yes, ARG1 activity can be targeted for therapeutic interventions. In certain diseases, such as cancer and immune-mediated disorders, inhibiting ARG1 can be beneficial. By blocking ARG1 activity, the depletion of arginine can be prevented, allowing for enhanced T cell function and immune responses. Additionally, targeting ARG1 in MDSCs can alleviate immunosuppression and improve anti-tumor immunity. Several approaches, including small molecule inhibitors and immunotherapies, are being explored to modulate ARG1 activity for therapeutic purposes.

Does ARG1 have any role in wound healing or tissue repair?

Yes, ARG1 is involved in wound healing and tissue repair processes. In certain immune cells, such as macrophages, ARG1 expression is upregulated during wound healing. ARG1-expressing macrophages contribute to tissue repair by promoting angiogenesis and collagen deposition. Additionally, ARG1-derived urea can support cell proliferation and tissue remodeling. However, the exact mechanisms and contributions of ARG1 in wound healing are still being studied.

Is there any relationship between the ARG1 protein and cardiovascular diseases?

Yes, there might be a link between ARG1 and cardiovascular diseases. Studies have suggested that ARG1 activity in blood vessels and endothelial cells may contribute to vascular dysfunction and hypertension. By modulating the availability of arginine and the production of nitric oxide, ARG1 can impact endothelial function and blood vessel dilation, which are important factors in cardiovascular health.

What other cellular pathways or proteins interact with ARG1?

ARG1 can interact with various cellular pathways and proteins. One important interaction is between ARG1 and nitric oxide synthase (NOS), particularly inducible NOS (iNOS). ARG1 and iNOS compete for the common substrate arginine, and their activities can reciprocally regulate each other. The balance between ARG1 and iNOS activity is critical for the production of arginine-derived metabolites, such as urea and nitric oxide, which have diverse physiological effects.

Are there any drugs targeting ARG1 being developed?

Yes, there is ongoing research to develop drugs targeting ARG1. For example, in cancer immunotherapy, scientists are exploring the use of ARG1 inhibitors to enhance anti-tumor immune responses. By blocking ARG1 activity in tumor-associated immune cells, the aim is to alleviate immunosuppression and enhance the efficacy of immune checkpoint inhibitors or other cancer therapies.

Are there any known pharmacological inhibitors of ARG1?

Yes, there are pharmacological inhibitors of ARG1 that have been identified and are under investigation. Some examples include nor-NOHA (N-omega-hydroxy-nor-L-arginine) and BEC (Bis-2-(5-phenylacetamido-1,3,4-thiadiazol-2-yl)ethyl sulfide). These inhibitors have shown promising results in preclinical studies and are being evaluated for their potential in treating diseases associated with aberrant ARG1 activity.

Can ARG1 activity be regulated by post-translational modifications?

Yes, ARG1 activity can be regulated by post-translational modifications, although the extent and significance of such modifications are still being investigated. For instance, phosphorylation of ARG1 on specific residues has been found to modulate its activity. Other post-translational modifications, such as acetylation and ubiquitination, may also influence ARG1 stability and function.

In which tissues or cell types is ARG1 expressed?

ARG1 is primarily expressed in the liver, although it can also be found in other tissues such as the kidneys, intestines, and immune cells, including macrophages. In these tissues, ARG1 plays a crucial role in regulating arginine metabolism and urea production.

Are there any natural compounds or dietary factors that can modulate ARG1 activity?

Yes, certain natural compounds and dietary factors have been found to modulate ARG1 activity. For instance, polyphenols, such as quercetin and resveratrol, have been shown to inhibit ARG1 activity. Dietary factors like high-protein diets can also affect ARG1 expression and activity. However, more research is needed to fully understand the extent of these modulatory effects and their therapeutic implications.