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exec

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Lepton

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  1. we have sephadex g-25, sephadex g-50 and sephadex g-75 resins. our protein is 20 Kda and we would like to desalt it for further processing. Can some one recommend which of these will be suitable. i.e which will cause less dilution and better desalting. we would be packing them in XK 16/40 column and use for desalting so what amount of sample can be desalted at a time. kindly suggest thanks
  2. We have been using SDS PAGE for quite some time for our recombinant protein Mw 20 kdA USING 15% Resolving and 4% stacking and tris glycine SDS Running buffer i.e laemelli system. is there any new methodology for SDS page that will increase resolution and help in getting clear sharp bands, any different buffer system or any such method. we do not want to use precast gels and cast our own gels. Also we use discontinuous Mode of buffer system. Any suggestions are welcome. regards
  3. Hello All, We are facing a peculiar problem. I have attached my SDS PAGE gel for reference. We get a pattern as if protein has spilled into adjacent well and the blank well (1st and last) also shows band. we have been performing the same method for same protein for about 7 yrs with no difficulty but from past 2-3 months are encountering this problem. we have tried preparing fresh reagents and do the test but same results. what can be the problem as while loading the protein does not spill, still this results is confusing. Can anyone throw some light or elaborate on this. Any help will be appreciated. Thanks in anticipation
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