Site-specific covalent labeling of His-tag fused proteins with a reactive Ni(II)-NTA probe.
A new method for covalent labeling of a His-tag fused protein with a small reactive probe was developed; this method is based on the complementary interaction between the His-tag and Ni(II)-NTA, which facilitates a nucleophilic reaction between a histidine residue of the tag and the electrophilic tosyl group of the Ni(II)-NTA probe by the proximity effect.
Uchinomiya
Sho-hei
SH
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura Campus, Kyoto, 615-8510, Japan.
Nonaka
Hiroshi
H
Fujishima
Sho-hei
SH
Tsukiji
Shinya
S
Ojida
Akio
A
Hamachi
Itaru
I
D001665:Binding Sites; D003374:Coumarins / Q000737:chemistry; D005456:Fluorescent Dyes / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D009532:Nickel / Q000737:chemistry*; D009571:Nitrilotriacetic Acid / Q000737:chemistry*; D009942:Organometallic Compounds / Q000737:chemistry*; D013194:Staining and Labeling
D003374:Coumarins; D005456:Fluorescent Dyes; D009942:Organometallic Compounds; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; D006639:Histidine; D009532:Nickel; C030123:coumarin; D009571:Nitrilotriacetic Acid