Estimated? ?size? ?of? ?prominent? ?band? ?in? ?lane? ?6? ?is? ?about? ?40kDa. 5.? ?The? ?molecular? ?mass? ?of? ?the? ?tagged? ?GST? ?protein? ?is? ?14kDa? ?viven? ?GST? ?=? ?26? ?kDa. 6.? ?Our? ?protein? ?purification? ?can? ?be? ?considered? ?to? ?have? ?moderate? ?success.

? ?Examining? F?? igure? ?1? ??wesee? ?lane? ?6? ?and? ?lane? ?7? ?show? ?similar? ?intensities? ?as? ?lane? ?10? ?(4ug)? ?protein,? ?which? ?is? ?suggestive? ?of? ?apurified? ?protein. 7.? ?Based? ?on? ?BSA? ?standards? ?the? ?total? ?amount? ?of? ?purified? ?protein? ?and? ?yield? ?can? ?be? ?close? ?to? ?40mg/l? ?(protein/? ?L? ?bacterial? ?culture).

? ?Lane? ?7? ?has? ?close? ?to? ?same? ?Rf? ?value? ?as? ?lane? ?10? ?and? ?can? ?beused? ?to? ?calculate? ?the? ?protein? ?mg/L? ?? ?because? ?we? ?know? ?lane? ?10? ?is? ?0.4ug/ul. 8.? ?Looking? ?at? ?the? ?vector? ?map? ?presented? ?earlier? ?in? ?the? ?lab? ?manual,? ?it? ?would? ?be? ?possible? ?to? ?removethe? ?GST? ?tag? ?from? ?a? ?protein? ?of? ?interest? ?with? ?a? ?restriction? ?digest? ?enzyme.? ?GST? ?is? ?covalently? ?placedon? ?the? ?cleavage? ?site? ?Bal? ?I? ?which? ?is? ?why? ?a? ?restriction? ?digest? ?enzyme. 9.

? ?Advantage? ?of? ?using? ?fusion? ?tag-based? ?affinity? ?protein? ?purification? ?is? ?at? ?the? ?end? ?a? ?completelypurified? ?protein? ?is? ?the? ?product.? ?The? ?application? ?of? ?fusion? ?tag-based? ?affinity? ?protein? ?purification? ?isto? ?express? ?recombinant? ?proteins? ?in? ?large? ?amounts? ?while? ?bound? ?to? ?a? ?tag,? ?and? ?ideal? ?for? ?pulldownexperiements. 

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