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Mouse Anti-ARG2 Recombinant Antibody (A10) (CBMAB-A3477-YC)

Provided herein is a Mouse monoclonal antibody against Human Arginase 2. The antibody can be used for immunoassay techniques, such as WB, IHC, ICC, IF, IHC-P.
See all ARG2 antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat, Pig, Cattle, Dog
Clone
A10
Antibody Isotype
IgA, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
Amino acids 304-335 near the C-terminus of Arg2 of human origin.
Specificity
Human, Mouse, Rat, Pig, Cattle, Dog
Antibody Isotype
IgA, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
arginase, type II
Introduction
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exists (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic funct
Entrez Gene ID
Human383
Dog480364
Rat29215
Monkey711033
UniProt ID
HumanP78540
DogE2R8N6
RatO08701
MonkeyH2Q8H7
Alternative Names
Arginase 2; EC 3.5.3.1; Kidney-Type Arginase; Non-Hepatic Arginase; Arginase, Type II; Type II Arginase; Arginase II; EC 3.5.3;
Function
May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune responses. Seems to be involved in negative regulation of the survival capacity of activated CD4+ and CD8+ T cells (PubMed:27745970).
May suppress inflammation-related signaling in asthmatic airway epithelium (PubMed:27214549).
May contribute to the immune evasion of H.pylori by restricting M1 macrophage activation and polyamine metabolism (By similarity).
In fetal dendritic cells may play a role in promoting immune suppression and T cell TNF-alpha production during gestation (PubMed:28614294).
Regulates RPS6KB1 signaling, which promotes endothelial cell senescence and inflammation and implicates NOS3/eNOS dysfunction (PubMed:22928666).
Can inhibit endothelial autophagy independently of its enzymatic activity implicating mTORC2 signaling (PubMed:25484082).
Involved in vascular smooth muscle cell senescence and apoptosis independently of its enzymatic activity (PubMed:23832324).
Since NOS is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase-2 plays a role in both male and female sexual arousal (PubMed:12859189).
Biological Process
Adaptive immune response Source: UniProtKB-KW
Arginine catabolic process to ornithine Source: GO_Central
Innate immune response Source: UniProtKB-KW
Negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process Source: Ensembl
Negative regulation of CD4-positive, alpha-beta T cell proliferation Source: Ensembl
Negative regulation of chemokine (C-C motif) ligand 4 production Source: Ensembl
Negative regulation of chemokine (C-C motif) ligand 5 production Source: Ensembl
Negative regulation of defense response to bacterium Source: Ensembl
Negative regulation of interleukin-13 production Source: Ensembl
Negative regulation of interleukin-17 production Source: Ensembl
Negative regulation of macrophage inflammatory protein 1 alpha production Source: Ensembl
Negative regulation of tumor necrosis factor production Source: UniProtKB
Negative regulation of type 2 immune response Source: Ensembl
Nitric oxide biosynthetic process Source: ProtInc
Positive regulation of cellular senescence Source: UniProtKB
Regulation of interleukin-1 beta production Source: Ensembl
Regulation of reactive oxygen species biosynthetic process Source: Ensembl
Striated muscle contraction Source: Ensembl
Urea cycle Source: Reactome
Ureteric bud development Source: Ensembl
Cellular Location
Mitochondrion

Dowling, J. K., Afzal, R., Gearing, L. J., Cervantes-Silva, M. P., Annett, S., Davis, G. M., ... & McCoy, C. E. (2021). Mitochondrial arginase-2 is essential for IL-10 metabolic reprogramming of inflammatory macrophages. Nature communications, 12(1), 1-14.

Wetzel, M. D., Stanley, K., Wang, W. W., Maity, S., Madesh, M., Reeves, W. B., & Awad, A. S. (2020). Selective inhibition of arginase-2 in endothelial cells but not proximal tubules reduces renal fibrosis. JCI insight, 5(19).

Hara, M., Torisu, K., Tomita, K., Kawai, Y., Tsuruya, K., Nakano, T., & Kitazono, T. (2020). Arginase 2 is a mediator of ischemia–reperfusion injury in the kidney through regulation of nitrosative stress. Kidney International, 98(3), 673-685.

Zhang, Y., Higgins, C. B., Fortune, H. M., Chen, P., Stothard, A. I., Mayer, A. L., ... & DeBosch, B. J. (2019). Hepatic arginase 2 (Arg2) is sufficient to convey the therapeutic metabolic effects of fasting. Nature communications, 10(1), 1-16.

i Líndez, A. A. M., Dunand-Sauthier, I., Conti, M., Gobet, F., Núñez, N., Hannich, J. T., ... & Reith, W. (2019). Mitochondrial arginase-2 is a cell‑autonomous regulator of CD8+ T cell function and antitumor efficacy. JCI insight, 4(24).

Ng, K. P., Manjeri, A., Lee, L. M., Chan, Z. E., Tan, C. Y., Tan, Q. D., ... & Ong, S. T. (2018). The arginase inhibitor Nω− hydroxy− nor− arginine (nor− NOHA) induces apoptosis in leukemic cells specifically under hypoxic conditions but CRISPR/Cas9 excludes arginase 2 (ARG2) as the functional target. Plos one, 13(10), e0205254.

Ochocki, J. D., Khare, S., Hess, M., Ackerman, D., Qiu, B., Daisak, J. I., ... & Simon, M. C. (2018). Arginase 2 suppresses renal carcinoma progression via biosynthetic cofactor pyridoxal phosphate depletion and increased polyamine toxicity. Cell metabolism, 27(6), 1263-1280.

Pandey, D., Nomura, Y., Rossberg, M. C., Hori, D., Bhatta, A., Keceli, G., ... & Romer, L. (2018). Hypoxia triggers SENP1 (Sentrin-Specific Protease 1) modulation of KLF15 (Kruppel-Like Factor 15) and transcriptional regulation of Arg2 (Arginase 2) in pulmonary endothelium. Arteriosclerosis, thrombosis, and vascular biology, 38(4), 913-926.

Zaytouni, T., Tsai, P. Y., Hitchcock, D. S., DuBois, C. D., Freinkman, E., Lin, L., ... & Kalaany, N. Y. (2017). Critical role for arginase 2 in obesity-associated pancreatic cancer. Nature communications, 8(1), 1-12.

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For research use only. Not intended for any clinical use.

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