Arginase 1/ARG1/liver Arginase Antibody - BSA Free Summary
Immunogen |
Arginase 1/ARG1/liver Arginase Antibody made from full length human Arginase 1 Recombinant protein. |
Localization |
Cytoplasm/Nucleus |
Predicted Species |
Bovine (90%), Rabbit (91%). Backed by our 100% Guarantee. |
Isotype |
IgG |
Clonality |
Polyclonal |
Host |
Rabbit |
Gene |
ARG1 |
Purity |
Immunogen affinity purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Flow Cytometry 5 - 10 ug/ml
- Immunocytochemistry/ Immunofluorescence 1:10 - 1:500
- Immunohistochemistry 1:100-1:1000
- Immunohistochemistry-Frozen 1:10 - 1:500
- Immunohistochemistry-Paraffin 1:100-1:1000
- Immunoprecipitation 1:10 - 1:500
- Knockdown Validated
- Simple Western
- Western Blot 1:1000-1:50000
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Reviewed Applications |
Read 1 Review rated 4 using NBP1-32731 in the following applications:
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Publications |
Read Publications using NBP1-32731 in the following applications:
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Reactivity Notes
Rat reactivity reported in scientific literature (PMID:32701588). Immunogen displays the following percentage of sequence identity for non-tested species: Porcine (89%).
Packaging, Storage & Formulations
Storage |
Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. |
Buffer |
PBS |
Preservative |
0.02% Sodium Azide |
Concentration |
1.0 mg/ml |
Purity |
Immunogen affinity purified |
Alternate Names for Arginase 1/ARG1/liver Arginase Antibody - BSA Free
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.
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Product General Protocols
View specific protocols for Arginase 1/ARG1/liver Arginase Antibody (NBP1-32731):
Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.
Video Protocols
FAQs for Arginase 1/ARG1/liver Arginase Antibody (NBP1-32731). (Showing 1 - 1 of 1 FAQs).
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Does the anti-arginase 1 antibody have any specificity towards Arginase II?
- NBP1-32731 has not been epitope mapped, and cross-reactivity with Arginase II has not been explicitly tested.As you are probably aware, ARG1 and ARG2 share about 60% homology with each other. Since this antibody has not been epitope mapped its hard to say whether this antibody will also detect ARG2. There are some stretches of conservation that are 15 AA long, so it is possible that ARG2 could be recognized with this antibody, especially considering it is a polyclonal antibody. We have 20 primary antibodies that target ARG1, so perhaps you could find one that has the immunogen listed here
Secondary Antibodies
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Isotype Controls
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