Arginase 1/ARG1/liver Arginase Antibody (OTI4E6) - Azide and BSA Free

Arginase 1 (ARG1), also known as liver arginase, is a metalloenzyme that is a member of the ureohydrolase superfamily and arginase family (1). ARG1 is known for its role in the urea cycle in catalyzing the conversion of L-arginine into urea and L-ornithine (1). Arginase has two distinct isoforms, with ARG1 being expressed primarily in the liver and ARG2 in extrahepatic tissues (1). Human ARG1 is synthesized as 322 amino acids (aa) in length with a theoretical molecular weight of 35 kDa (1,2). Three ARG1 monomers can form a highly active homotrimer of 105 kDa (1). A key structural feature of the arginase protein is the binuclear magnesium (Mn2+) ions at its core (1).

Arginase and nitric oxidase synthase (NOS) compete for the same L-arginine substrate, creating a delicate balance between pathways (1). Furthermore, bioavailability of L-arginine and ARG1 expression has been implicated in several pathologies including vascular disease, neuronal disease, cardiovascular disease, immune dysfunction, inflammation, and cancer (1,3-5). For instance, ARG1 functions as a macrophage marker, defining the M2 population, while inducible nitric oxide synthase (iNOS) characterizes the M1 population; impaired M1/M2 polarization and changes in ARG1 expression is observed in diseases such as arteriogenesis, asthma, pulmonary fibrosis, and inflammatory bowel disease (1,3). In humans, arginase deficiency, known as argininemia, is an autosomal recessive metabolic disorder characterized by elevated ammonia (hyperammonemia) levels and arginine accumulation (6). Given that many arginase-associated diseases are characterized by upregulation in expression of ARG1, ARG2, or both, arginase inhibitors are currently being studied as a potential therapeutic approach (1,4).

References

1. S Clemente, G., van Waarde, A., F Antunes, I., Domling, A., & H Elsinga, P. (2020). Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. International Journal of Molecular Sciences. https://doi.org/10.3390/ijms21155291

2. Uniprot (P05089)

3. Kieler, M., Hofmann, M., & Schabbauer, G. (2021). More than just protein building blocks: How amino acids and related metabolic pathways fuel macrophage polarization. The FEBS Journal. Advance online publication. https://doi.org/10.1111/febs.15715

4. Shosha, E., Fouda, A. Y., Narayanan, S. P., Caldwell, R. W., & Caldwell, R. B. (2020). Is the Arginase Pathway a Novel Therapeutic Avenue for Diabetic Retinopathy?. Journal of Clinical Medicine. https://doi.org/10.3390/jcm9020425

5. Correale J. (2021). Immunosuppressive Amino-Acid Catabolizing Enzymes in Multiple Sclerosis. Frontiers in Immunology. https://doi.org/10.3389/fimmu.2020.600428

6. Morales, J. A., & Sticco, K. L. (2020). Arginase Deficiency. In StatPearls. StatPearls Publishing.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Array NBP2-70204

• Arginase 1/ARG1/liver Arginase Antibodies
• Arginase 1/ARG1/liver Arginase ELISA Kit
• Arginase 1/ARG1/liver Arginase Kit
• Arginase 1/ARG1/liver Arginase Lysate
• Arginase 1/ARG1/liver Arginase Proteins
• Arginase 1/ARG1/liver Arginase Proteins and Enzyme