Mouse anti-Human sapiens (Human) ARG1 Monoclonal Antibody

Function

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

Subcellular Location

Cytoplasm; Cytoplasmic granule

Disease Association

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, intellectual disability, hypotonia, ataxia and progressive spastic quadriplegia. [The disease is caused by variants affecting the gene represented in this entry]

Tissue Specificity

Within the immune system initially reported to be selectively expressed in granulocytes (polymorphonuclear leukocytes [PMNs]) (PubMed:15546957). Also detected in macrophages mycobacterial granulomas (PubMed:23749634). Expressed in group2 innate lymphoid cells (ILC2s) during lung disease (PubMed:27043409)

Subunit

Homotrimer (PubMed:16141327, PubMed:17469833, PubMed:17562323, PubMed:18802628, PubMed:2241902). Interacts with CMTM6 (PubMed:28813417)

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1

• Haraguchi Y. et al. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. — Proc. Natl. Acad. Sci. U.S.A. (1987)
• Takiguchi M. et al. Human liver-type arginase gene: structure of the gene and analysis of the promoter region. — Nucleic Acids Res. (1988)
• Lee Y.T. et al. PubMed: CI-2VJ84T121CKTB (JAN-)
• Kalnine N. et al. Cloning of human full-length CDSs in BD Creator(TM) system donor vector. (MAY-)
• Mungall A.J. et al. The DNA sequence and analysis of human chromosome 6. — Nature (2003)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Ikemoto M. et al. Expression of human liver arginase in Escherichia coli. Purification and properties of the product. — Biochem. J. (1990)
• Munder M. et al. Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity. — Blood (2005)