Phosphorylation of specific serine or threonine residues is an important post-translational modification for regulating the activity of most proteins. Stimulation of a variety of cell signaling pathways activates the receptor and non-receptor ser/thr kinases that mediate these protein modifications. Antibodies that can detect phosphoserine or phosphothreonine residues are excellent tools for characterizing changes in the post-translational state of a broad range of phosphorylated proteins. Immunoprecipitation of proteins of interest followed by detection of phosphoserine or phosphothreonine using anti-phosphoserine antibody is commonly used to correlate changes in phosphorylation state with alterations in protein activity.
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Su, KH et al. (2019) Molecular Cell 76:116. (WB: human HEK293 cells)
Malleske, DT et al. (2018) Stem Cells. 36(12):1905. (WB: human Epithelial cells)
Xiao, N. et al. (2019) FASEB J. 33(1):163-174. (IP: Hek293 cells)
Su, KH et al. (2016) Nat Cell Biol. 18(5):527. (WB: human HEK293 cells)
Osma-Garcia, I.C. et al. (2015) Eur J Immunol. doi: 10.1002 (WB: mouse macrophages)
Fester, L. et al. (2015) JSBMB S0960-0760(15)30109. (WB: Hippocampal neurons)
Paul, NR et al. (2015) J Cell Biol. 210(6):1013. (WB: human ovarian cancer cells)
Morinaga, J. et al. (2013) AJP Renal Phys. 305(2)F173. (WB: Normal rat Kidney Fibroblast)
This kit contains: