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Ten optimal spectral bands were selected using the algorithm, with six out the selected bands within the same near-infrared spectral region.

Bands were selected using the rectangle tool and the background was cropped.

Bands were selected using the Volume Rectangle Tool, and the 'Adjusted Volume Intensity mm value' was used as an arbitrary unit of intensity.

Protein bands were selected using the lasso tool copied to a new layer, and mean pixel intensity determined for both total protein (protein from all eleven fractions of the gradient) and for DRM-localised protein (protein in the flotillin-2-positive fractions).

Commensurate number of spectral components in each sub-band was selected (using psychoacoustic model) and their parameters were vector quantized.

The bands in each lane were selected using Quantity One software, and there were twelve, nineteen and twenty two bands in lane 1 (Gl), lane 2 (Av) and lane 3 (RS), respectively.

Equivalent band areas across samples were selected using the volume rectangle tool.

Next, the lanes were selected using the rectangle tool and band intensity profiles plotted using the gel analysis functions.

Wavelengths for excitation and emission of the MDCC were selected using monochromators with a 1-nm band pass width.

mRFP tagged proteins were excited by a 561 nm laser line and the emission was selected using a band-pass filter between 580 680 nm.

Immunofluorescence was examined on an Olympus FV1000 confocal microscope (Olympus, Japan) using a 63×/1.4 oil immersion objective with a pinhole at airy 1. GFP tagged proteins were excited by a 488 nm laser line and the emission was selected using a band-pass filter between 500 550 nm.