Both　CIEF　and　MALDI-MS　are　frequently　used　in　protein　analysis,　but　hyphenation　of　the　two　has　not　been　investigated　proportionally.　One　of　the　major　reasons　is　that　the　additives　(such　as　carrier　ampholytes　and　detergent)　in　CIEF　severely　suppress　the　MALDI-MS　signal,　which　hampers　the　hyphenation　of　the　two.　In　this　paper,　we　develop　a　simple　means　to　alleviate　the　above　signal-suppressing　effect.　We　first　deposit　1　mu　L　of　water　onto　a　MALDI-MS　target,　deliver　a　fraction　of　CIEF-separated　protein　(similar　to　0.1　mu　L)　to　the　water　droplet,　evaporate　the　solvent,　add　0.5　mu　L　of　MALDI　matrix　to　the　sample　spot,　dry　the　matrix　and　move　the　target　plate　to　a　MALDI-TOF-MS　for　mass　spectrum　measurement.　We　optimize　the　droplet　volume　and　the　laser-ablation　region.　Under　the　optimized　conditions,　we　improve　the　SIN　by　two-　to　tenfold.　We　also　apply　this　method　for　2-D　separations　of　standard　proteins　and　apolipoprotein　A-I,　a　membrane　protein　expressed　in　Escherichia　colt　cells.