Copper iodide stains

Root, D. D. and Reisler, E. (1989) Copper iodide staining of protein blots on nitrocellulose membranes. Anal. Biochem. 181, 250-253. 

Copper iodide stains proteins on nitrocellulose and nylon with a sensitivity comparable to silver stain in the gel. Root and Reisler (1989) claim that this stain is inexpensive, quick (5 minutes), can easily be removed again, and maintains the immunoreactivity of the blotted proteins. 

For blots with protein amounts less than 50 ng/band, the Ponceau red staining is the method of choice. Aurodye and copper iodide can be used for protein amoimts less than 50 ng/band. Li et al. (1989) compare different protein staining methods. Ponceau red stains protein on nitrocellulose blots (see Table 1.2). The staining is reversible and allows subsequent immu-nostaining. The blot is incubated for 1 to 2 minutes at RT in Ponceau red (2% in 3% trichloroacetic acid), and the surplus stain is then washed away with water. 

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