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Arginase 1/ARG1/liver Arginase Assay Kit (Colorimetric)

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Product Details

Summary
Reactivity Hu, Mu, RtSpecies Glossary
Applications Func, NULL
Suitable Sample Type
Enzyme preparations, serum, plasma, tissue culture etc
Standard Curve Range
0.3 to 20 U/L
Sensitivity
0.3 U/L

Order Details

Arginase 1/ARG1/liver Arginase Assay Kit (Colorimetric) Summary

Description
Arginase Assay Kit is a quantitative colorimetric arginase determination.
Standard Curve Range
0.3 to 20 U/L
Sensitivity
0.3 U/L
Assay Type
Colorimetric
Sample Volume
40 uL
Kit Type
Assay Kit (Colorimetric)
Gene
ARG1

Applications/Dilutions

Dilutions
  • Functional
  • Quantification
Publications
Read Publications using KA1609.

Reactivity Notes

Rat reactivity reported in scientific literatures (PMID: 26315997 and 24440670).

Packaging, Storage & Formulations

Storage
Storage of components varies. See protocol for specific instructions.

Kit Components

Components
  1. Arginine Buffer (pH 9.5)
  2. Mn Solution
  3. Reagent A
  4. Reagent B
  5. Urea standard (50 mg/dL)

Notes

This product is produced by and distributed for Abnova, a company based in Taiwan.

Alternate Names for Arginase 1/ARG1/liver Arginase Assay Kit (Colorimetric)

  • AI
  • ARG1
  • Arginase 1
  • arginase, liver
  • Arginase-1
  • EC 3.5.3.1
  • EC:3.5.3.1
  • Liver Arginase
  • Liver-type arginase
  • PGIF
  • Type I Arginase

Background

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.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Kits are guaranteed for 6 months from date of receipt.

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Publications for Arginase 1/ARG1/liver Arginase Kit (KA1609)(21)


Showing Publications 1 - 10 of 21. Show All 21 Publications.
Publications using KA1609 Applications Species
Trotta MC, Gesualdo C, Petrillo F et al. Serum Iba-1, GLUT5, and TSPO in Patients With Diabetic Retinopathy: New Biomarkers for Early Retinal Neurovascular Alterations? A Pilot Study Translational vision science & technology 2022-03-02 [PMID: 35285861]
Maryam S, Mahmoud J, Ali B et al. Preparation of liposomes containing IFN-gamma and their potentials in cancer immunotherapy: In vitro and in vivo studies in a colon cancer mouse model. Life Sci. 2020-10-20 [PMID: 33096119]
Weinhage T, Dabritz J, Brockhausen A et al. Granulocyte Macrophage Colony-Stimulating Factor-Activated CD39+/CD73+ Murine Monocytes Modulate Intestinal Inflammation via Induction of Regulatory T Cells. CMGH Jul 1 2015
Jiajun C, Shiqi C, Renjie L et al. Blockade of Cycloxygenase-2 ameliorates sepsis induced immune-suppression by regulating myeloid-derived suppressor cells. Int Immunopharmacol. 2022-01-07 [PMID: 35008007]
Houjun X, Shasha L, Xiong L et al. Autophagic adaptation to oxidative stress alters peritoneal residential macrophage survival and ovarian cancer metastasis. JCI Insight. 2020-09-17 [PMID: 32780724]
WC Lee, PY Hsu, HY Hsu Stem cell factor produced by tumor cells expands myeloid-derived suppressor cells in mice Sci Rep, 2020-07-09;10(1):11257. 2020-07-09 [PMID: 32647215]
Xiaojing Z, Wen W, Fang C et al. Myeloid-derived Suppressor Cells Exert Immunosuppressive Function on the T Helper 2 in Mice Infected With Echinococcus Granulosus. Exp Parasitol. 2020-05-22 [PMID: 32446699]
Kubota T, Inoue M, Kubota N et al. Downregulation of macrophage Irs2 by hyperinsulinemia impairs IL-4-indeuced M2a-subtype macrophage activation in obesity. Nat Commun. 2018-11-19 [PMID: 30451856]
Sikkema AH, Stoffels JMJ, Wang P et al. Fibronectin aggregates promote features of a classically and alternatively activated phenotype in macrophages. J Neuroinflammation 2018-08-02 [PMID: 30071854]
Ochocki JD, Khare S, Hess M et al. Arginase 2 Suppresses Renal Carcinoma Progression via Biosynthetic Cofactor Pyridoxal Phosphate Depletion and Increased Polyamine Toxicity. Cell Metab 2018-05-10 [PMID: 29754953]
Show All 21 Publications.

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Bioinformatics

Gene Symbol ARG1