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>   首页   >   产品   >   一抗   >   信号转导   >   Anti-Ceruloplasmin Picoband Antibody   

Anti-Ceruloplasmin Picoband Antibody

     
  • 1 - Anti-Ceruloplasmin Picoband Antibody ABO12538
    Western blot analysis of Ceruloplasmin expression in 22RV1 whole cell lysates (lane 1) and A549 whole cell lysates (lane 2). Ceruloplasmin at 122KD was detected using rabbit anti- Ceruloplasmin Antigen Affinity purified polyclonal antibody at0.5 μg/mL. The blot was developed using chemiluminescence (ECL) method .
  • 2 - Anti-Ceruloplasmin Picoband Antibody ABO12538
    Ceruloplasmin was detected in paraffin-embedded sections of human liver cancer tissues using rabbit anti- Ceruloplasmin Antigen Affinity purified polyclonal antibody (Catalog # ABO12538) at 1 ??g/mL. The immunohistochemical section was developed using SABC method .
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P
Primary Accession P00450
Host Rabbit
Reactivity Human
Clonality Polyclonal
Format Lyophilized
Description Rabbit IgG polyclonal antibody for Ceruloplasmin(CP) detection. Tested with WB, IHC-P in Human.
Reconstitution Add 0.2ml of distilled water will yield a concentration of 500ug/ml.
Additional Information
Gene ID 1356
Other Names Ceruloplasmin, 1.16.3.1, Ferroxidase, CP
Calculated MW 122219 Da
Application Details Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat

Western blot, 0.1-0.5 µg/ml, Human
Subcellular Localization Secreted. Colocalizes with GCP1 in secretory intracellular compartments. .
Tissue Specificity Expressed by the liver and secreted in plasma.
Source Eukaryota
Protein Name Ceruloplasmin
Contents Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
Immunogen E. coli-derived human Ceruloplasmin recombinant protein (Position: K20-M259). Human Ceruloplasmin shares 80.8% and 79.6% amino acid (aa) sequence identity with mouse and rat Ceruloplasmin, respectively.
Purification Immunogen affinity purified.
Cross Reactivity No cross reactivity with other proteins.
Storage At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name CP (HGNC:2295)
Function Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo- transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Acts as an inhibitor of the peroxidase activity of MPO (By similarity). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150).
Cellular Location Secreted. Note=Colocalizes with GCP1 in secretory intracellular compartments {ECO:0000250|UniProtKB:P13635}
Tissue Location Expressed by the liver and secreted in plasma.
Research Areas

BACKGROUND

Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene. It is mapped to 3q23-q25. The protein encoded by this gene is a metalloprotein that binds most of the copper in plasma and is involved in the peroxidation of Fe(II)transferrin to Fe(III) transferrin. Mutations in this gene cause aceruloplasminemia, which results in iron accumulation and tissue damage, and is associated with diabetes and neurologic abnormalities. Two transcript variants, one protein-coding and the other not protein-coding, have been found for this gene.

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