Skip to main content

Arginase 1/ARG1/liver Arginase Antibody (ARG1/7514R) [Janelia Fluor® 549]

Novus Biologicals, part of Bio-Techne | Catalog # NBP3-20711JF549

Recombinant Monoclonal Antibody
Novus Biologicals, part of Bio-Techne

Key Product Details

Species Reactivity

Human

Applications

Immunohistochemistry-Paraffin

Label

Janelia Fluor 549

Antibody Source

Recombinant Monoclonal Rabbit IgG Kappa Clone # ARG1/7514R

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Product Specifications

Immunogen

Recombinant human Arginase 1/ARG1/liver Arginase protein fragment (aa300-400) (Exact sequence is proprietary)

Localization

Cytoplasm.

Clonality

Monoclonal

Host

Rabbit

Isotype

IgG Kappa

Applications

Application
Recommended Usage

Immunohistochemistry-Paraffin

Optimal dilutions of this antibody should be experimentally determined.
Application Notes
Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Purification

Protein A or G purified

Formulation

50mM Sodium Borate

Preservative

0.05% Sodium Azide

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C in the dark.

Background: Arginase 1/ARG1

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.

Long Name

Liver-Type Arginase

Alternate Names

AI, ARG1, Arginase-1, Liver Arginase, PGIF, Type I Arginase

Gene Symbol

ARG1

Additional Arginase 1/ARG1 Products

Product Documents

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Product Specific Notices



Sold under license from the Howard Hughes Medical Institute, Janelia Research Campus.

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.

Loading...
Loading...
Loading...
Loading...