Near-infrared fluorescence detection of ATP-biotin-mediated phosphoprotein labeling.
Detection of phosphoproteins plays an important role in understanding protein function in cellular signalling pathways. Improved methods for identification and quantification of phosphoproteins are research priorities. Near-infrared (NIR) fluorescence detection of a gamma-modified ATP-biotin analog was used to detect protein phosphorylation, using both model kinase substrates and mammalian cell lysates. NIR signal intensity was dependent on substrate and ATP-biotin concentrations.
Gao
Xiaofei
X
Center for Infectious Disease Research and Vaccinology, South Dakota State University, Box 2175, 1119 North Campus Drive, Brookings, SD 57007, USA.
Schutz-Geschwender
Amy
A
Hardwidge
Philip R
PR
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001710:Biotin / Q000378:metabolism*; D002457:Cell Extracts; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D005453:Fluorescence; D006367:HeLa Cells; D006801:Humans; D010455:Peptides / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D016315:Proto-Oncogene Proteins c-abl / Q000378:metabolism; D019265:Spectroscopy, Near-Infrared; D013194:Staining and Labeling; D013379:Substrate Specificity
D002457:Cell Extracts; D010455:Peptides; D010750:Phosphoproteins; D001710:Biotin; D000255:Adenosine Triphosphate; D016315:Proto-Oncogene Proteins c-abl; D017868:Cyclic AMP-Dependent Protein Kinases