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We recently bought ceruloplasmin, want to use to find its cofactor by x-ray based methods. My question is whether copper ions are stably bound with ceruloplasmin or only less chance for such a binding ( lost during purification )
I would like to get your opinion and suggestions
Asked on Oct 21 2013
For ab77930 Human Ceruloplasmin protein, the copper ions are stably bound as long as you do not change the buffer. The buffer this was lyophilized from is as follows:
Buffer: Lyophilized from 50 mM Potassium Phosphate, pH 6.8, 100 mM Potassium Chloride, 20 mM E-amino-n-caproic acid and 5 mM EDTA.
NOTE: Exposure to sodium (in the form of sodium chloride, sodium phosphate, sodium azide as well as other sodium containing reagents) should be avoided, as ceruloplasmin may precipitate under these conditions. Buffers that ceruloplasmin is exposed to should be pH adjusted with potassium hydroxide.
The following references may also be helpful:
The Inhibition of Caeruloplasmin by Azide, G. Curzon, Biochem. J. (1966) 100, 295.
Purification and Characterization of Undegraded Human Ceruplasmin, M. Noyer, etal, Analytical Biochemistry 102, 450-458 (1980).
Sam WasherAbcam Scientific Support
Answered on Oct 21 2013