Simple bioseparations using self-cleaving elastin-like polypeptide tags.
We introduce a new method for the purification of recombinant proteins expressed in Escherichia coli using self-cleaving elastin-like polypeptide (ELP) fusion tags without the need for affinity chromatography or proteolytic tag removal. Using this method we obtained high purity, activity and reasonable yields for ten diverse target proteins.
Banki
Mahmoud Reza
MR
Department of Chemical Engineering, A213 E-QUAD, Princeton University, Princeton, New Jersey 08544, USA.
Feng
Liang
L
Wood
David W
DW
D005591:Chemical Fractionation / Q000379:methods*; D004549:Elastin / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005590:Fractional Precipitation; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D015202:Protein Engineering / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification*; D013194:Staining and Labeling / Q000379:methods; D014462:Ultrafiltration / Q000379:methods*
D010455:Peptides; D011993:Recombinant Fusion Proteins; D004549:Elastin