= Western blot transfer
<Western blot transfer> moves separated <proteins> out of the gel onto a <Western blot membrane>, using an <electric field> across the gel thickness. Maintaining close contact preserves the lane pattern. Contact gaps, incomplete removal from the gel and passage through the receiving sheet can change how much <protein> is retained.
The original 1979 experiment pressed a wetted, $0.45\,\mu\mathrm m$-pore <nitrocellulose Western blot membrane> against the gel between scouring pads and plastic pipette-tray grids, held by elastic bands. The <urea>-gel assembly faced the <cathode> in acidic solution, with $6\,\mathrm{V/cm}$ applied for one hour; the <SDS-PAGE> variant reversed polarity and used a <glycine>/<methanol> <buffer solution>. Stained gel/blot pairs checked pattern preservation. Corresponding labelled <ribosome> <protein> spots from two gels were compared through <radioactive decay> readouts after combustion. The stained gel remaining after transfer supplied a removal check; a second receiving sheet revealed breakthrough on overloading. These tests supported recovery for the examined <urea>-gel <proteins>, within experimental variation, while the <SDS-PAGE> results showed unequal staining recovery. Preserved band positions therefore did not establish universal quantitative transfer. <Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications by Harry Towbin and others>[Towbin, Staehelin and Gordon, pp. 4350–4352: Electrophoretic Blotting Procedures, Figure 1, Figures 2–3 and Table 1]{ref}
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