Arginase 1/ARG1/liver Arginase Antibody (CL0186) - Azide and BSA Free Summary
| Description |
Novus Biologicals Mouse Arginase 1/ARG1/liver Arginase Antibody (CL0186) - Azide and BSA Free (NBP2-14787) is a monoclonal antibody validated for use in IHC, WB and Simple Western. All Novus Biologicals antibodies are covered by our 100% guarantee. |
| Immunogen |
This antibody was generated using a recombinant protein sequence of P05089, with the exact immunogen sequence remaining proprietary. |
| Isotype |
IgG1 |
| Clonality |
Monoclonal |
| Host |
Mouse |
| Gene |
ARG1 |
| Purity |
Protein A purified |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
| Dilutions |
- Immunohistochemistry-Paraffin 1:2500 - 1:5000
- Simple Western 1:20
- Western Blot 1 ug/ml
|
| Application Notes |
For IHC-Paraffin, HIER pH 6 retrieval is recommended.
In Simple Western only 10 - 15 uL of the recommended dilution is used per data point. Separated by Size-Wes, Sally Sue/Peggy Sue. |
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
| Buffer |
Lyophilized from a 0.2 um filtered solution in PBS with Trehalose |
| Preservative |
No Preservative |
| Concentration |
LYOPH |
| Purity |
Protein A purified |
| Reconstitution Instructions |
Centrifuge the vial of lyophilized antibody at 12,000 x g for 20 seconds. Reconstitute by adding sterile, distilled water to achieve a final antibody concentration of 1mg/ml. |
Alternate Names for Arginase 1/ARG1/liver Arginase Antibody (CL0186) - Azide and 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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