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Mouse Anti-ARG1 Recombinant Antibody (658922) (CBMAB-1134-CN)

This product is a mouse antibody that recognizes ARG1 of human. The antibody 658922 can be used for immunoassay techniques such as: FC, CyTOF.
See all ARG1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
658922
Antibody Isotype
IgG2b
Application
FC

Basic Information

Immunogen
E. coli-derived recombinant human Arginase 1/ARG1 Met1-Lys322.
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
FC2.5 µg/10^6 cells

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

Format
Lyophilized
Buffer
PBS, Trehalose.
Preservative
None
Concentration
LYOPH
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 1
Introduction
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. The protein is a key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.
Entrez Gene ID
383
UniProt ID
P05089
Alternative Names
arginase-1; arginase, liver; liver-type arginase; type I arginase; EC 3.5.3.1
Function
Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.
Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (PubMed:15546957, PubMed:16709924, PubMed:19380772).
In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (By similarity).
In humans, the immunological role in the monocytic/macrophage/dendritic cell (DC) lineage is unsure.
Biological Process
Adaptive immune response Source: UniProtKB-KW
Aging Source: Ensembl
Arginine catabolic process Source: ProtInc
Arginine catabolic process to ornithine Source: GO_Central
Cellular response to dexamethasone stimulus Source: Ensembl
cellular response to glucagon stimulus Source: Ensembl
Cellular response to hydrogen peroxide Source: Ensembl
Cellular response to interleukin-4 Source: Ensembl
Cellular response to lipopolysaccharide Source: Ensembl
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Collagen biosynthetic process Source: Ensembl
Defense response to protozoan Source: Ensembl
Innate immune response Source: UniProtKB-KW
Liver development Source: Ensembl
Lung development Source: Ensembl
Mammary gland involution Source: Ensembl
Maternal process involved in female pregnancy Source: Ensembl
Negative regulation of activated T cell proliferation Source: Ensembl
Negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKB
Negative regulation of T cell proliferation Source: UniProtKB
Negative regulation of T-helper 2 cell cytokine production Source: Ensembl
Neutrophil degranulation Source: Reactome
Positive regulation of endothelial cell proliferation Source: Ensembl
Positive regulation of neutrophil mediated killing of fungus Source: UniProtKB
Regulation of L-arginine import Source: Ensembl
Response to amine Source: Ensembl
Response to amino acid Source: Ensembl
Response to axon injury Source: Ensembl
Response to cadmium ion Source: Ensembl
Response to drug Source: Ensembl
Response to herbicide Source: Ensembl
Response to manganese ion Source: Ensembl
Response to methylmercury Source: Ensembl
Response to selenium ion Source: Ensembl
Response to vitamin A Source: Ensembl
Response to vitamin E Source: Ensembl
Response to zinc ion Source: Ensembl
Urea cycle Source: Reactome
Cellular Location
Cytoplasm; Cytoplasmic granule. Localized in azurophil granules of neutrophils (PubMed:15546957).
Involvement in disease
Argininemia (ARGIN): A rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia and progressive spastic quadriplegia.

Hannemann, J., Rendant-Gantzberg, L., Zummack, J., Hillig, J., Eilermann, I., & Böger, R. (2021). Single Nucleotide Polymorphisms in the Arginase 1 and 2 Genes Are Differentially Associated with Circulating l-Arginine Concentration in Unsupplemented and l-Arginine–Supplemented Adults. The Journal of Nutrition, 151(4), 763-771.

Derakhshani, A., Hemmat, N., Asadzadeh, Z., Ghaseminia, M., Shadbad, M. A., Jadideslam, G., ... & Baradaran, B. (2021). Arginase 1 (Arg1) as an Up-Regulated Gene in COVID-19 Patients: A Promising Marker in COVID-19 Immunopathy. Journal of Clinical Medicine, 10(5), 1051.

Gao, Z. W., Li, L., Huang, Y. Y., Zhao, C. Q., Xue, S. J., Chen, J., ... & Su, X. (2021). Vagal-α7nAChR signaling is required for lung anti-inflammatory responses and arginase 1 expression during an influenza infection. Acta Pharmacologica Sinica, 1-11.

Yokoi, K., Nakajima, Y., Yasui, T., Yoshino, M., Yoshikawa, T., Kurahashi, H., & Ito, T. (2021). Novel ARG1 variants identified in a patient with arginase 1 deficiency. Human Genome Variation, 8(1), 1-4.

Ma, C., Hunt, J. B., Selenica, M. L. B., Sanneh, A., Sandusky-Beltran, L. A., Watler, M., ... & Lee, D. C. (2020). Arginase 1 Insufficiency Precipitates Amyloid-β Deposition and Hastens Behavioral Impairment in a Mouse Model of Amyloidosis. Frontiers in Immunology, 11.

Zhao, G., Chen, W., He, J., Cui, C., Zhao, L., Zhao, Y., ... & Kong, L. (2020). Analysis of cyclooxygenase 2, programmed cell death ligand 1, and arginase 1 expression in human pituitary adenoma. World Neurosurgery, 144, e660-e673.

Czystowska-Kuzmicz, M., Sosnowska, A., Nowis, D., Ramji, K., Szajnik, M., Chlebowska-Tuz, J., ... & Golab, J. (2019). Small extracellular vesicles containing arginase-1 suppress T-cell responses and promote tumor growth in ovarian carcinoma. Nature communications, 10(1), 1-16.

Diez‐Fernandez, C., Rüfenacht, V., Gemperle, C., Fingerhut, R., & Häberle, J. (2018). Mutations and common variants in the human arginase 1 (ARG1) gene: Impact on patients, diagnostics, and protein structure considerations. Human mutation, 39(8), 1029-1050.

Asrani, K. H., Cheng, L., Cheng, C. J., & Subramanian, R. R. (2018). Arginase I mRNA therapy–a novel approach to rescue arginase 1 enzyme deficiency. RNA biology, 15(7), 914-922.

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

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