Anti-Arginase-2, mitochondrial Arg2 Antibody Picoband® Fluoro488 Conjugated

ARG2 (arginase, type II) encodes a 355-amino acid polypeptide.  Using Northern blotting and RT-PCR,   Vockley et al. (1996)   found that  ARG2  is expressed as a 1.5-kb mRNA in a wide variety of tissues, with highest levels of expression in prostate, brain, and kidney.  By PCR analysis of somatic cell hybrid panels, fluorescence in situ hybridization, and radiation hybrid analysis,   the  ARG2 gene is mapped to 14q24.1-q24.3. ARG2  may be inducible and may be essential in the regulation of nitric oxide synthesis by modulating local arginine concentrations. Gotoh et al. (1996)   showed that  ARG2  mRNA and nitric oxide synthase (NOS) mRNA were coinduced by lipopolysaccharide in a macrophage-like cell line. Arginase II has been implicated in the regulation of the arginine/ornithine concentrations in the cell. The mitochondrial location of  ARG2  and its coinduction with ornithine aminotransferase and involvement with proline biosynthesis in lactating rat mammary gland had led to the inference that  ARG2  is involved in biosynthetic functions, as opposed to the metabolic ones of the urea cycle.

A synthetic peptide corresponding to a sequence at the N-terminus of human Arg2, different from the related mouse sequence by three amino acids and from the related rat sequence by two amino acids.

Expressed most strongly in kidney and prostate, much less strongly in the brain, skeletal muscle, placenta, lung, mammary gland, macrophage, uterus, testis and gut, but apparently not in the liver, heart and pancreas.

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 NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders. .

1. Deignan, J. L., Livesay, J. C., Yoo, P. K., Goodman, S. I., O'Brien, W. E., Iyer, R. K., Cederbaum, S. D., Grody, W. W. Ornithine deficiency in the arginase double knockout mouse. Molec. Genet. Metab. 89: 87-96, 2006. 2. Gotoh, T., Sonoki, T., Nagasaki, A., Terada, K., Takiguchi, M., Mori, M. Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line. FEBS Lett. 395: 119-122, 1996. 3. Vockley, J. G., Jenkinson, C. P., Shukla, H., Kern, R. M., Grody, W. W., Cederbaum, S. D. Cloning and characterization of the human type II arginase gene. Genomics 38: 118-123, 1996.