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Purified Mouse Anti-Arginase I
Purified Mouse Anti-Arginase I

Western blot analysis of Arginase I on a mouse liver lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-arginase I antibody.

Purified Mouse Anti-Arginase I

Immunofluorescence staining of mouse macrophages.

Western blot analysis of Arginase I on a mouse liver lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-arginase I antibody.

Immunofluorescence staining of mouse macrophages.

Product Details
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BD Transduction Laboratories™
Mouse (QC Testing), Rat, Fly (Tested in Development)
Mouse IgG1
Human Arginase I aa. 53-207
Western blot (Routinely Tested), Immunofluorescence, Immunohistochemistry (Tested During Development), Immunoprecipitation (Not Recommended)
35 kDa
250 µg/ml
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.

Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

Western blot:  Please refer to

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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Antibody Details
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19/Arginase I

Arginase converts arginine into urea plus ornithine, the final step in urea synthesis. Two different isoforms (I&II) have been isolated with approximately 60% homology at the nucleotide level. While type II is present in many tissues, Arginase I is expressed exclusively in liver. In cultured macrophages, as well as in vivo, Arginase I is induced with nitric oxide synthase (NOS) and the arginase I transactivator C/EBPβ in response to lipopolysaccharide. This response occurs in a dose and time-dependent manner. While the mRNA for NOS appears as early as 2h after treatment, mRNA levels for arginase I peak after twelve hours of lipopolysaccharide treatment. Since the synthesis of nitric oxide by NOS requires arginine, the delayed induction of arginase I may be necessary for the regulation of NOS activity.

This antibody is routinely tested by western blot analysis. Othe applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.

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Format Details
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Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
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Citations & References
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Development References (5)

  1. Chang CI, Zoghi B, Liao JC, Kuo L. The involvement of tyrosine kinases, cyclic AMP/protein kinase A, and p38 mitogen-activated protein kinase in IL-13-mediated arginase I induction in macrophages: its implications in IL-13-inhibited nitric oxide production. J Immunol. 2000; 165(4):2134-2141. (Biology: Western blot). View Reference
  2. Dizikes GJ, Grody WW, Kern RM, Cederbaum SD. Isolation of human liver arginase cDNA and demonstration of nonhomology between the two human arginase genes. Biochem Biophys Res Commun. 1986; 141(1):53-59. (Biology). View Reference
  3. Haraguchi Y, Takiguchi M, Amaya Y, Kawamoto S, Matsuda I, Mori M. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Proc Natl Acad Sci U S A. 1987; 84(2):412-415. (Biology). View Reference
  4. Morrison AC, Correll PH. Activation of the stem cell-derived tyrosine kinase/RON receptor tyrosine kinase by macrophage-stimulating protein results in the induction of arginase activity in murine peritoneal macrophages. J Immunol. 2002; 168(2):853-860. (Biology: Western blot). View Reference
  5. Sonoki T, Nagasaki A, Gotoh T. Coinduction of nitric-oxide synthase and arginase I in cultured rat peritoneal macrophages and rat tissues in vivo by lipopolysaccharide. J Biol Chem. 1997; 272((6):3689-3693. (Biology). View Reference
View All (5) View Less
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