|Application ||WB, IHC-P|
|Description||Rabbit IgG polyclonal antibody for Ceruloplasmin(CP) detection. Tested with WB, IHC-P in Mouse;Rat.|
|Reconstitution||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Other Names||Ceruloplasmin, 220.127.116.11, Ferroxidase, Cp|
|Calculated MW||121151 MW KDa|
|Application Details||Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Mouse, Rat, By Heat|
Western blot, 0.1-0.5 µg/ml, Mouse
|Subcellular Localization||Secreted. Colocalizes with GCP1 in secretory intracellular compartments. .|
|Tissue Specificity||Expressed in many tissues, including liver, eye and brain. .|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.|
|Immunogen||E. coli-derived mouse Ceruloplasmin recombinant protein (Position: R20-M258). Mouse Ceruloplasmin shares 80.8% and 91.2% amino acid (aa) sequence identity with human 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.|
|Function||Ceruloplasmin is a 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. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).|
|Cellular Location||Secreted. Note=Colocalizes with GCP1 in secretory intracellular compartments.|
|Tissue Location||Expressed in many tissues, including liver, eye and brain.|
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Provided below are standard protocols that you may find useful for product applications.
CeruloplasminÂ (orÂ caeruloplasmin) is aÂ ferroxidaseÂ enzymeÂ that in humans is encoded by theÂ CPÂ 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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