GW20074F
Anti-Ceruloplasmin antibody produced in chicken
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-Ferroxidase
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About This Item
Recommended Products
biological source
chicken
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human
manufacturer/tradename
Genway 15-288-20074F
technique(s)
indirect ELISA: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CP(1356)
Application
Anti-Ceruloplasmin antibody produced in chicken is suitable for indirect ELISA and western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme encoded by the CP gene in humans. It is a ferroxidase present in the cerebrospinal fluid (CSF). CP is associated with promoting the function of integrin binding, signaling and cell adhesion. The CP level is correlated negatively and indirectly with inflammation as well as fibrosis stages in male patients with chronic hepatitis B (CHB). It decreases the nitric oxide bioavailability in blood and is associated with cardiovascular disease (CVD).
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Marco Barbariga et al.
The Journal of biological chemistry, 289(6), 3736-3748 (2013-12-25)
Asparagine deamidation occurs spontaneously in proteins during aging; deamidation of Asn-Gly-Arg (NGR) sites can lead to the formation of isoAsp-Gly-Arg (isoDGR), a motif that can recognize the RGD-binding site of integrins. Ceruloplasmin (Cp), a ferroxidase present in the cerebrospinal fluid
Razvan T Dadu et al.
Circulation. Heart failure, 6(5), 936-943 (2013-07-19)
Ceruloplasmin (Cp) decreases nitric oxide bioavailability in blood and has been associated with cardiovascular disease (CVD) in clinical studies. We assessed the associations between Cp and incident heart failure (HF), death, and CVD in the Atherosclerosis Risk in Communities (ARIC)
Lingli Jiang et al.
American journal of physiology. Gastrointestinal and liver physiology, 301(5), G877-G886 (2011-08-20)
The Menkes copper ATPase (Atp7a) and metallothionein (Mt1a) are induced in the duodenum of iron-deficient rats, and serum and hepatic copper levels increase. Induction of a multi-copper ferroxidase (ceruloplasmin; Cp) has also been documented. These findings hint at an important
Aneta Jończy et al.
Metallomics : integrated biometal science, 11(6), 1079-1092 (2019-04-24)
Jackson toxic milk mutant mice (tx-J) carrying a missense mutation in the Atp7b gene are animal models of the Wilson disease. In both the Wilson patients and the tx-J mice, mutations in the ATP7B/Atp7b gene lead to disturbances in copper
Perungavur N Ranganathan et al.
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 25(4), 687-695 (2012-02-22)
Discovered over a decade ago, hephaestin (Heph) has been implicated as a ferroxidase (FOX) vital for intestinal iron absorption. Stringent structural or kinetic data derived from purified, native protein is however lacking, leading to the hypothesis that an alternate, undiscovered
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