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Arginase, Liver (ARG1) (AA 53-207) antibody

Details for Product No. ABIN968128, Supplier: Login to see
Antigen
  • SI:zC146F4.4 (novel protein with NUDIX domain)
  • si:ch211-146f4.3
  • argi1
  • AI
  • AI256583
  • Arg-1
  • PGIF
Epitope
AA 53-207
68
44
27
11
9
7
6
5
4
3
3
3
2
1
1
1
1
1
1
1
1
1
Reactivity
Fly (Calliphora), Mouse (Murine), Rat (Rattus)
169
58
51
20
11
8
6
1
1
Host
Mouse
140
48
29
7
4
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
12
12
8
7
7
6
2
1
1
1
1
1
1
1
1
1
1
1
Application
Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
170
110
46
37
22
16
16
11
8
3
3
3
1
1
1
1
1
1
1
1
1
Supplier
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Immunogen Human Arginase I aa. 53-207
Clone 19-Arginase I
Isotype IgG1
Cross-Reactivity Mouse (Murine), Rat (Rattus), Fruit Fly (Drosophila melanogaster)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us 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.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Arginase I (ARG1 Antibody Abstract)
Background 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/EBPbeta 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.
Molecular Weight 35 kDa
Pathways
Comment

Related Products: ABIN968543, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Store undiluted at -20° C.
Supplier Images
Western Blotting (WB) image for anti-Arginase, Liver (ARG1) (AA 53-207) antibody (ABIN968128) Western blot analysis of Arginase I on a mouse liver lysate. Lane 1: 1:1000, lane 2: ...
Immunofluorescence (IF) image for anti-Arginase, Liver (ARG1) (AA 53-207) antibody (ABIN968128) Immunofluorescence staining of mouse macrophages.
 image for anti-Arginase, Liver (ARG1) (AA 53-207) antibody (ABIN968128) anti-Arginase, Liver (ARG1) (AA 53-207) antibody (Image 3)
Product cited in: Morrison, Correll: "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." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 168, Issue 2, pp. 853-60, 2002 (PubMed).

Chang, Zoghi, Liao et al.: "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." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 165, Issue 4, pp. 2134-41, 2000 (PubMed).

Sonoki, Nagasaki, Gotoh et al.: "Coinduction of nitric-oxide synthase and arginase I in cultured rat peritoneal macrophages and rat tissues in vivo by lipopolysaccharide." in: The Journal of biological chemistry, Vol. 272, Issue 6, pp. 3689-93, 1997 (PubMed).

Dizikes, Grody, Kern et al.: "Isolation of human liver arginase cDNA and demonstration of nonhomology between the two human arginase genes." in: Biochemical and biophysical research communications, Vol. 141, Issue 1, pp. 53-9, 1987 (PubMed).

Haraguchi, Takiguchi, Amaya et al.: "Molecular cloning and nucleotide sequence of cDNA for human liver arginase." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, Issue 2, pp. 412-5, 1987 (PubMed).