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

Details zu Produkt Nr. ABIN968127, Anbieter: Anmelden zum Anzeigen
Antigen
  • SI:zC146F4.4 (novel protein with NUDIX domain)
  • si:ch211-146f4.3
  • argi1
  • AI
  • AI256583
  • Arg-1
  • PGIF
  • arginase 1
  • arginase
  • Arginase-1
  • arginase, liver
  • L-arginase
  • arg1
  • PGTG_16455
  • argi1
  • ARG1
  • Arg1
Epitop
AA 53-207
70
42
18
18
10
7
7
7
5
5
3
3
3
2
2
2
1
1
1
1
1
1
1
1
1
1
Reaktivität
Fly (Calliphora), Maus, Ratte (Rattus)
197
80
71
24
16
14
8
5
3
3
2
2
1
1
Wirt
Maus
159
48
41
10
4
Klonalität (Klon)
Monoklonal ()
Konjugat
Unkonjugiert
13
13
10
8
8
7
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Applikation
Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
203
120
46
43
36
21
21
13
5
4
3
2
2
2
1
1
1
1
1
1
Optionen
Hersteller
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Hersteller Produkt- Nr.
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Immunogen Human Arginase I aa. 53-207
Klon 19-Arginase I
Isotyp IgG1
Kreuzreaktivität Maus, Ratte (Rattus), Fruchtfliege (Drosophila melanogaster)
Produktmerkmale 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.
Reinigung The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Andere Bezeichnung Arginase I (ARG1 Antibody Abstract)
Hintergrund 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.
Molekulargewicht 35 kDa
Pathways Cellular Response to Molecule of Bacterial Origin
Kommentare

Related Products: ABIN968543, ABIN967389

Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Konzentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Konservierungsmittel Sodium azide
Vorsichtsmaßnahmen This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung -20 °C
Informationen zur Lagerung Store undiluted at -20° C.
Bilder des Herstellers
Western Blotting (WB) image for anti-Arginase, Liver (ARG1) (AA 53-207) antibody (ABIN968127) 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 (ABIN968127) Immunofluorescence staining of mouse macrophages.
Produkt verwendet 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, Kuo: "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, Takiguchi, Takeya, Matsuzaki, Mori: "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, Cederbaum: "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, Kawamoto, Matsuda, Mori: "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).

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