| Field | Specification |
|---|---|
| Assay Time | |
| Detection Method | |
| Product Type | |
| Sample Type(s) | Enzyme preparations, serum, plasma, tissue culture etc |
| Shipping | |
| Species | |
| Storage |
Overview
For quantitative determination of arginase activity and screen for its inhibitors. The assay uses OD430nm for signal readout. Compatible sample input includes Enzyme preparations, serum, plasma, tissue culture etc. Typical stated assay timing is 2 hrs.
Key elements and design rationale
- Readout format: OD430nm supports plate-based signal acquisition and consistent comparison across matched samples.
- Sample compatibility: The stated sample scope includes Enzyme preparations, serum, plasma, tissue culture etc, which is useful when aligning matrix type with calibration and control design.
- Analytical range context: The supplied specifications include a stated detection limit of 1 U/L (0.3 U/L for 2 hr reaction) for interpreting low-signal samples.
- Feature emphasis: Sensitive and accurate. Detection limit: 0.3 U/L for 2 hr arginase reaction in 96-well assay format.
Additional feature notes highlight Simple and high-throughput. The procedure involves incubation of the provided substrate with the sample in a microplate followed by the addition of the coloring reagent. Can be readily automated as a high-throughput assay for thousands of samples per day. Available format information for this listing includes 100 Tests.
Biological background
This product is centered on measurement of arginase (100t) within the matrices described for the assay. In practice, datasets from this type of format are typically interpreted by comparing relative signal, activity, or abundance across matched control and experimental groups rather than relying on a single value in isolation. Careful alignment of sample matrix, incubation window, and calibration strategy is important when comparing results across plates, operators, or study days.
More details
ARGINASE(L-arginine ureohydrolase EC 3.5.3.1) is present in mammals and plants. In humans, arginase is expressed predominantly in the liver, and to lesser degrees in breast, kidney, testes, salivary glands, epidermis and erythrocytes. Arginase catalyzes the conversion of arginine to ornithine and urea, completing the last step in the urea cycle. Arginase activity is a key diagnostic indicator. Increased levels of arginase activity in blood have been associated with liver damage. Hyperargininemia due to arginase deficiency is an inherited autosomal recessive disease. Simple, direct and automation-ready procedures for measuring arginase activity in biological samples are highly desirable in Research and Drug Discovery. BioAssay Systems arginase assay kit provides a sensitive and convenient method for arginase activity determination. The method utilizes a chromogen that forms a colored complex specifically with urea produced in the arginase reaction. The intensity of the color is directly proportional to the arginase activity in the sample.
Detection method
Colorimetric (OD 430 nm).
Detection limit and analytical sensitivity
Reported detection limit: 1 U/L (0.3 U/L for 2 hr reaction).
Procedures and timing
Stated procedure or timing information: 2 hrs.
Research relevance and current trends
- Plate-based quantification and side-by-side group comparison remain central use cases for this assay format.
- The product notes emphasize multi-sample throughput, making it relevant for screening-oriented and larger batch comparison studies.
- The description supports intervention-focused study designs in which researchers compare baseline and perturbed conditions.
Common research applications
- Quantify arginase (100t) in enzyme preparations, serum, plasma by OD430 nm readout.
- Compare treatment or phenotype groups using matched enzyme preparations, serum, plasma handling.
- Monitor time-course or pre/post changes in enzyme preparations, serum, plasma across study conditions.
Interpretation is usually strongest when signal changes are assessed alongside matrix-matched controls, replicate agreement, and the assay's stated analytical window.
Notes for experimental interpretation
- Matrix composition, background signal, and sample handling can influence apparent response; compare like-with-like whenever possible.
- Use appropriate blanks, controls, and replicate wells to distinguish biological differences from plate, reagent, or handling variability.
What are the best samples, serum or plasma? And with or without heparin?
Wash 5-10 x105 cells and resuspend cell pellet in 100 μL lysis buffer containing 0.4% Triton X-100, 25 mM Tris-HCl (pH 7.5) and 1 mM MnSO4 (10 μL of the provided Mn Solution). Optionally, activate arginase by heating for 10 min at 55-60°C. For serum samples we found the heating step unnecessary, but we have not tested cell or tissue samples. Centrifuge for 2 minutes at 14,000 rpm on a table centrifuge and use clear supernatant in arginase assay.
I see in your protocol that you don’t heat the sample what is normally done in the literature. Is you protocol different? Should I heat my samples to activate the enzyme?
We tried to heat the enzyme (purified enzyme and serum samples) in the assay buffer and found no significant difference as compared to no heating. Therefore our protocol does not include the heating step.
For laboratories requiring additional technical capacity, we provide scientific support services including assay execution, method guidance, product sourcing, and customization to align the assay with specific experimental objectives. If you need assistance selecting the appropriate kit configuration, adapting the workflow to your application, or identifying related research services, please click Talk to a Scientist, email support@biohippo.com, or review our Research Services; a member of our scientific team will follow up with recommendations tailored to your study.
Semen cuscutae administration improves hepatic lipid metabolism and adiposity in high fat diet-induced obese mice
Moon, J et al (2019). Semen cuscutae administration improves hepatic lipid metabolism and adiposity in high fat diet-induced obese mice. Nutrients, 11(12). Assay: Arginase in mouse cells and tissue lysates.
Metformin inhibits the function of granulocytic myeloid-derived suppressor cells in tumor-bearing mice
Xu, P et al (2019). Metformin inhibits the function of granulocytic myeloid-derived suppressor cells in tumor-bearing mice. Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie, 120, 109458. Assay: Arginase in mouse cells.
Green tea polyphenol egcg attenuates mdscs-mediated immunosuppression through canonical and non-canonical pathways in a 4t1 murine breast cancer model
Xu, P et al (2020). Green tea polyphenol egcg attenuates mdscs-mediated immunosuppression through canonical and non-canonical pathways in a 4t1 murine breast cancer model. Nutrients, 12(4). Assay: Arginase in mouse cell lysates.
Chinese yellow rice wine processing with reduced ethyl carbamate formation by deleting transcriptional regulator dal80p in saccharomyces cerevisiae
Wei, T et al (2020). Chinese yellow rice wine processing with reduced ethyl carbamate formation by deleting transcriptional regulator dal80p in saccharomyces cerevisiae. Molecules, 25(16), 3580. Assay: Arginase in saccharomyces cerevisiae cells.
Chitinase 3-like 1 protein plays a critical role in respiratory syncytial virus-induced airway inflammation
Kim, MJ et al (2019). Chitinase 3-like 1 protein plays a critical role in respiratory syncytial virus-induced airway inflammation. Allergy, 74(4), 685-697. Assay: Arginase in mouse bronchoalveolar lavage fluid and lung lysates.
Methylprednisolone alleviates multiple sclerosis by expanding myeloid-derived suppressor cells via glucocorticoid receptor β and S100A8/9 up-regulation
Wang, Z et al (2020). Methylprednisolone alleviates multiple sclerosis by expanding myeloid-derived suppressor cells via glucocorticoid receptor β and S100A8/9 up-regulation. Journal of Cellular and Molecular Medicine. Assay: Arginase in human serum.
Olfactory ecto-mesenchymal stem cell-derived exosomes ameliorate murine Sjogren?s syndrome by modulating the function of myeloid-derived suppressor cells
Rui, K et al (2021). Olfactory ecto-mesenchymal stem cell-derived exosomes ameliorate murine Sjogren?s syndrome by modulating the function of myeloid-derived suppressor cells. Cellular & Molecular Immunology, 18(2), 440-451. Assay: Arginase in mouse serum.
Mesenchymal stem cell enhances the function of mdscs in experimental sjogren syndrome
Tian, J et al (2020). Mesenchymal stem cell enhances the function of mdscs in experimental sjogren syndrome. Frontiers in Immunology, 11. Assay: Arginase in mouse cells.
High glucose contributes to the polarization of peritoneal macrophages to the M2 phenotype in vivo and in vitro
Lin, J et al (2020). High glucose contributes to the polarization of peritoneal macrophages to the M2 phenotype in vivo and in vitro. Molecular Medicine Reports, 22(1), 127-134. Assay: Arginase in mouse cell lysates.
Early posttransplant mobilization of monocytic myeloid-derived suppressor cell correlates with increase in soluble immunosuppressive factors and predicts cancer in kidney recipients
Utrero-Rico, A et al (2020). Early posttransplant mobilization of monocytic myeloid-derived suppressor cell correlates with increase in soluble immunosuppressive factors and predicts cancer in kidney recipients. Transplantation, 104(12), 2599-2608. Assay: Arginase in human serum.
Characterization of ovine monocyte activity when cultured with Haemonchus contortus larvae in vitro
Shepherd, E et al (2020). Characterization of ovine monocyte activity when cultured with Haemonchus contortus larvae in vitro. Parasite Immunology, 42(11), e12773. Assay: Arginase in sheep monocytes.
Preparation of polymer microspheres capable for pioglitazone release to modify macrophages function
Momotori, N et al (2019). Preparation of polymer microspheres capable for pioglitazone release to modify macrophages function. Regenerative Therapy, 11, 131-138. Assay: Arginase in mouse cells.
Arginase 1 insufficiency precipitates amyloid-β deposition and hastens behavioral impairment in a mouse model of amyloidosis
Ma, C et al (2021). Arginase 1 insufficiency precipitates amyloid-β deposition and hastens behavioral impairment in a mouse model of amyloidosis. Frontiers in Immunology, 11. Assay: Arginase in mouse cell lysates.
Bone metastasis is associated with acquisition of mesenchymal phenotype and immune suppression in a model of spontaneous breast cancer metastasis
Monteran, L et al (2020). Bone metastasis is associated with acquisition of mesenchymal phenotype and immune suppression in a model of spontaneous breast cancer metastasis. Scientific Reports, 10(1), 13838. Assay: Arginase in mouse cell lysates.
Synthetic dna delivery of an engineered arginase enzyme can modulate specific immunity in vivo
Khoshnejad, M et al (2020). Synthetic dna delivery of an engineered arginase enzyme can modulate specific immunity in vivo. Molecular Therapy – Methods & Clinical Development, 18, 652-663. Assay: Arginase in mouse serum and cellular supernatant of transfected human embryonic kidney (HEK) 293T cells.
Circulating cd14+hla-dr-/low myeloid-derived suppressor cells as potential biomarkers for the identification of psoriasis tcm blood-heat syndrome and blood-stasis syndrome
Sun, S et al (2020). Circulating cd14+hla-dr-/low myeloid-derived suppressor cells as potential biomarkers for the identification of psoriasis tcm blood-heat syndrome and blood-stasis syndrome. Evidence-Based Complementary and Alternative Medicine: ECAM, 2020, 4582459. Assay: Arginase in human serum.
Polymorphonuclear-mdscs facilitate tumor regrowth after radiation by suppressing cd8+ t cells
Zhang, J et al (2020). Polymorphonuclear-mdscs facilitate tumor regrowth after radiation by suppressing cd8+ t cells. International Journal of Radiation Oncology, Biology, Physics. Assay: Arginase in mouse.
Botanical Drug Puerarin Attenuates 6-Hydroxydopamine(6-OHDA)-Induced Neurotoxicity via UpregulatingMitochondrial Enzyme Arginase-2
Zhao. J et al (2016). Botanical Drug Puerarin Attenuates 6-Hydroxydopamine(6-OHDA)-Induced Neurotoxicity via UpregulatingMitochondrial Enzyme Arginase-2. Mol Neurobiol. 53(4):2200-11. Assay: Arginase in rat pheochromocytoma cells.
Arginase promotes endothelial dysfunction and hypertension in obese rats
Johnson, FK et al (2015). Arginase promotes endothelial dysfunction and hypertension in obese rats. Obesity (Silver Spring). 23(2):383-90. Assay: Arginase in obese and lean zucker rats plasma.
A2B Adenosine Receptors Prevent Insulin Resistance by Inhibiting Adipose Tissue Inflammation via Maintaining Alternative Macrophage Activation
Csoka, B et al (2014). A2B Adenosine Receptors Prevent Insulin Resistance by Inhibiting Adipose Tissue Inflammation via Maintaining Alternative Macrophage Activation. Diabetes. 63(3):850-66. Assay: Arginase in rat adipose tissue.
Immunosuppression through constitutively activated NF-kB signalling in human ovarian cancer and its reversal by an NF-kB inhibitor
Nishio, H et al (2014). Immunosuppression through constitutively activated NF-kB signalling in human ovarian cancer and its reversal by an NF-kB inhibitor. Br J Cancer. 110(12):2965-74. Assay: Arginase in human epithelial cells.
Role of Metabolic Environment on Nitric Oxide Mediated Inhibition of Neointimal Hyperplasia in Type 1 and Type 2 Diabetes
Rodriguez, MP et al (2014). Role of Metabolic Environment on Nitric Oxide Mediated Inhibition of Neointimal Hyperplasia in Type 1 and Type 2 Diabetes. Nitric Oxide. 36:67-75. Assay: Arginase in lean zucker rats plasma.
Elevated levels of NO are localized to distal airways in asthma
Anderson JT, et al (2011). Elevated levels of NO are localized to distal airways in asthma. Free Radic Biol Med. 50(11):1679-88. Assay: Arginase in human bronchial fluids.
human NKT cells direct the differentiation of myeloid APCs that regulate T cell responses via expression of programmed cell death ligands
Hegde S, et al (2011). human NKT cells direct the differentiation of myeloid APCs that regulate T cell responses via expression of programmed cell death ligands. J Autoimmun. 37(1):28-38. Assay: Arginase in human cells.
A CD36-dependent pathway enhances macrophage and adipose tissue inflammation and impairs insulin signalling
Kennedy DJ, et al (2011). A CD36-dependent pathway enhances macrophage and adipose tissue inflammation and impairs insulin signalling. Cardiovasc Res. 89(3):604-13. Assay: Arginase in mouse plasma.
Functional characterization of human Cd33+ And Cd11b+ myeloid-derived suppressor cell subsets induced from peripheral blood mononuclear cells co-cultured with a diverse set of human tumor cell lines
Lechner MG, et al (2011). Functional characterization of human Cd33+ And Cd11b+ myeloid-derived suppressor cell subsets induced from peripheral blood mononuclear cells co-cultured with a diverse set of human tumor cell lines. J Transl Med. 9:90. Assay: Arginase in human cells.
Paired immunoglobin-like receptor-B regulates the suppressive function and fate of myeloid-derived suppressor cells
Ma, G et al (2011). Paired immunoglobin-like receptor-B regulates the suppressive function and fate of myeloid-derived suppressor cells. Immunity 34(3):385-95. Assay: Arginase in mouse macrophages.
Inhibition profile of Leishmania mexicana arginase reveals differences with human arginase I
Riley E, et al (2011). Inhibition profile of Leishmania mexicana arginase reveals differences with human arginase I. Int J Parasitol. 41(5):545-52. Assay: Arginase in human protein extracts.
Pivotal Advance: Tumor-mediated induction of myeloid-derived suppressor cells and M2-polarized macrophages by altering intracellular PGE2 catabolism in myeloid cells
Eruslanov E, et al (2010). Pivotal Advance: Tumor-mediated induction of myeloid-derived suppressor cells and M2-polarized macrophages by altering intracellular PGE2 catabolism in myeloid cells. J Leukoc Biol.88(5):839-48. Assay: Arginase in macrophages.
Azithromycin alters macrophage phenotype and pulmonary compartmentalization during lung infection with Pseudomonas
Feola DJ, et al (2010). Azithromycin alters macrophage phenotype and pulmonary compartmentalization during lung infection with Pseudomonas. Antimicrob Agents Chemother. 54(6):2437-47. Assay: Arginase in mouse cell lysates.
Direct detection of diverse metabolic changes in virally transformed and tax-expressing cells by mass spectrometry
Sripadi P, et al (2010). Direct detection of diverse metabolic changes in virally transformed and tax-expressing cells by mass spectrometry. PLoS One 5(9):e12590. Assay: Arginase in human cell line.
Elevated mitochondrial reactive oxygen species generation affects the immune response via hypoxia-inducible factor-1alpha in long-lived Mclk1+/- mouse mutants
Wang D, et al (2010). Elevated mitochondrial reactive oxygen species generation affects the immune response via hypoxia-inducible factor-1alpha in long-lived Mclk1+/- mouse mutants. J Immunol. 184(2):582-90. Assay: Arginase in mouse tissue.
Modulators of arginine metabolism support cancer immunosurveillance
Capuano G, et al (2009). Modulators of arginine metabolism support cancer immunosurveillance. BMC Immunol. 10:1. Assay: Arginase in mouse CD11b+ cells.
Altered expression of 15-hydroxyprostaglandin dehydrogenase in tumor-infiltrated CD11b myeloid cells: a mechanism for immune evasion in cancer
Eruslanov E, et al (2009). Altered expression of 15-hydroxyprostaglandin dehydrogenase in tumor-infiltrated CD11b myeloid cells: a mechanism for immune evasion in cancer. J Immunol. 182(12):7548-57. Assay: Arginase in mouse cell lysates.
Successful immunotherapy with IL-2/anti-CD40 induces the chemokine-mediated mitigation of an immunosuppressive tumor microenvironment
Weiss, JM et al (2009). Successful immunotherapy with IL-2/anti-CD40 induces the chemokine-mediated mitigation of an immunosuppressive tumor microenvironment. PNAS 106(46):19455-60. Assay: Arginase in mouse tumor tissue.
Zinc supplementation decreases oxidative stress, incidence of infection, and generation of inflammatory cytokines in sickle cell disease patients
Bao B, et al (2008). Zinc supplementation decreases oxidative stress, incidence of infection, and generation of inflammatory cytokines in sickle cell disease patients. Transl Res. 152(2):67-80. Assay: Arginase in human tissue.
Comparative real-time PCR and enzyme analysis of selected gender-associated molecules in Schistosoma japonicum
Moertel L, et al (2008). Comparative real-time PCR and enzyme analysis of selected gender-associated molecules in Schistosoma japonicum. Parasitology 135(5):575-83. Assay: Arginase in snail protein extracts.
Azithromycin alters macrophage phenotype
Murphy BS, et al (2008). Azithromycin alters macrophage phenotype. J Antimicrob Chemother. 61(3):554-60. Assay: Arginase in human cells.
Burn injury-induced alterations in wound inflammation and healing are associated with suppressed hypoxia inducible factor-1alpha expression
Schwacha MG, et al (2008). Burn injury-induced alterations in wound inflammation and healing are associated with suppressed hypoxia inducible factor-1alpha expression. Mol Med. 14(9-10):628-33. Assay: Arginase in mouse wound homogenates.
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