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      Purified Mouse Anti-Ceruloplasmin
      Purified Mouse Anti-Ceruloplasmin
      Western blot analysis of Ceruloplasmin on a rat testis lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti-Ceruloplasmin antibody.
      Purified Mouse Anti-Ceruloplasmin

      Immunofluorescence staining of SK-BR-3 cells (Human breast adenocarcinoma; ATCC HTB-30).

      Purified Mouse Anti-Ceruloplasmin Purified Mouse Anti-Ceruloplasmin
      Western blot analysis of Ceruloplasmin on a rat testis lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti-Ceruloplasmin antibody.

      Immunofluorescence staining of SK-BR-3 cells (Human breast adenocarcinoma; ATCC HTB-30).

      Product Details
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      BD Transduction Laboratories™
      Rat (QC Testing), Human, Mouse (Tested in Development)
      Mouse IgG1
      Mouse ceruloplasmin aa. 233-355
      Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
      132 kDa
      250 µg/ml
      Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
      RUO


      Preparation And Storage

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

      Western blot:  Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml

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      Product Notices

      1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
      2. Please refer to www.bdbiosciences.com/us/s/resources 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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      611489 Rev. 1
      Antibody Details
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      8/Ceruloplasmin

      Ceruloplasmin (CP) is a copper-containing glycoprotein that carries approximately 90% of plasma copper. CP contains six copper atom binding sites and is prone to transfer its copper atoms to tissues, however it is not essential for copper transport. In cultured endothelial cells, CP release of copper in the cytosol inhibits nitric oxide synthase activation, and this may be important for regulating vascular tone in blood vessels. In addition to its copper binding role, CP has also been shown to have ferroxidase activity, which involves conversion of ferrous to ferric iron. The iron metabolism disorder aceruloplasminemia results from mutations in CP and is characterized by massive iron deposits in liver, pancreas, brain, retina, and other tissues. CP is expressed in the liver, the splenic reticuloendothelial system, the bronchiolar epithelium of the lung, and the retina and brain. The cell-specific expression of CP in neural tissues may account for the neuropathologies associated with aceruloplaminemia, while the wide expression pattern of CP may demonstrate its importance in the regulation of copper and iron levels in many tissues.

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

      611489 Rev. 1
      Format Details
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      Purified
      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.
      Purified
      611489 Rev.1
      Citations & References
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      Development References (5)

      1. Attieh ZK, Mukhopadhyay CK, Seshadri V, Tripoulas NA, Fox PL. Ceruloplasmin ferroxidase activity stimulates cellular iron uptake by a trivalent cation-specific transport mechanism. J Biol Chem. 1999; 274(2):1116-1123. (Biology). View Reference
      2. Bianchini A, Musci G, Calabrese L. Inhibition of endothelial nitric-oxide synthase by ceruloplasmin. J Biol Chem. 1999; 274(29):20265-20270. (Biology). View Reference
      3. Kaplan J, O'Halloran TV. Iron metabolism in eukaryotes: Mars and Venus at it again. Science. 1996; 271(5255):1510-1512. (Biology). View Reference
      4. Klomp LW, Farhangrazi ZS, Dugan LL, Gitlin JD. Ceruloplasmin gene expression in the murine central nervous system. J Clin Invest. 1996; 98(1):207-215. (Biology). View Reference
      5. Mukhopadhyay CK, Attieh ZK, Fox PL. Role of ceruloplasmin in cellular iron uptake. Science. 1998; 279(5351):714-717. (Biology). View Reference
      View All (5) View Less
      611489 Rev. 1

      Please refer to Support Documents for Quality Certificates


      Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described


      Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

      For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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