Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NB100-59740] - (0.003ug/ml) staining of Mouse (A) and Rat (B) Liver lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.
WB: Approx. 37 kDa band observed in mouse and rat liver lysates (calculated MW of 35 kDa band according to NP_058830.2 and 34.8kDa according to Mouse NP_031508.1). Primary incubation 1 hour at room temperature. IHC-F usage is reported in scientific literature (PMID: 24089194). Use in ICC/IF reported in scientific literature (PMID 28246332). Use in Flow Cytometry reported in (PMID: 24089194). Use in IHC reported in scientific literature (PMID: 23207546).
Theoretical MW
37 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using NB100-59740 in the following applications:
Human reactivity reported in scientific literature (PMID: 28246332).
Packaging, Storage & Formulations
Storage
Store at -20C. Avoid freeze-thaw cycles.
Buffer
Tris saline (20 mM Tris pH 7.3, 150 mM NaCl), 0.5% BSA
Preservative
0.02% Sodium Azide
Concentration
0.5 mg/ml
Purity
Immunogen affinity purified
Alternate Names for Arginase 1/ARG1/liver Arginase Antibody
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. Primary Antibodies are guaranteed for 1 year from date of receipt.
Publications for Arginase 1/ARG1/liver Arginase Antibody (NB100-59740)(17)
We have publications tested in 3 confirmed species: Human, Mouse, Rat.
We have publications tested in 8 applications: FLOW, ICC/IF, IF/IHC, IHC-Fr, Immunocytochemistry/ Immunofluorescence, Immunohistochemistry-Frozen, WB, Western Blot.
Zhou J, Zhang C, Yang X et al. Study on the effect of sevoflurane on the cognitive function of aged rats based on the activation of cortical microglia Ibrain 2021-12-01 (WB, Rat)
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