Home » Product » Phospho-Tag™ Phosphoprotein Gel Stain


Phospho-Tag™ Phosphoprotein Gel Stain


Phospho-Tag™ Phosphoprotein Gel Stain is a high sensitive fluorescent stain designed for selectively detecting phosphoproteins in polyacrylamide gels. This stain contains a phospho-tag™ group, which allows direct, in-gel detection of phosphate groups attached to tyrosine, serine, or threonine residues, without the need for antibodies or radioisotopes. The stain can be used with standard SDS-polyacrylamide gels or with 2-D gels.


  • High sensitivity. Detect as little as 1 ng phosphoprotein.
  • Simple and fast staining.
  • Compatibility with standard laboratory equipment.
  • Wide linear detection range. At least three orders of magnitude.
  • Compatible with downstream analysis: Compatible with MS and sequencing.
  • Stable: Stable at room temperature for 1 year.


Protein gel stain

To Order

Buy Catalog # Product Name Description Size List Price
P005A Phospho-Tag™ Phosphoprotein Gel Stain Phosphoprotein gel stain 500 mL $200
P005B Phospho-Tag Phosphoprotein Destain Solution  Destain solution 500 mL $55



Protocol (PDF): P005A
MSDS (PDF):  P005A

Cited Reference:

 Protein Targets of Inositol Pyrophosphate (5-IP7) in the parasite Trypanosoma cruzi
Brian S. Mantilla, Nathaniel Brown, Dorothea Fiedler, Roberto Docampo
bioRxiv 2020.01.09.900860; doi: https://doi.org/10.1101/2020.01.09.900860

cMyBPC phosphorylation modulates the effect of omecamtiv mecarbil on myocardial force generation
Ranganath Mamidi, Joshua B. Holmes, Chang Yoon Doh, Katherine L. Dominic, Nikhil Madugula, and Julian E. Stelzer
J. Gen. Physiol. 2021, 153, 7, e202012816. https://doi.org/10.1085/jgp.202012816

In-Depth Characterization of the Clostridioides difficile Phosphoproteome to Identify Ser/Thr Kinase Substrates
Transito Garcia-Garcia, Thibaut Douche, Quentin Giai Gianetto, Sandrine Poncet, Nesrine El Omrani, Wiep Klaas Smits, Elodie Cuenot, Mariette Matondo, and Isabelle Martin-Verstraete
Mol Cell Proteomics, 2022, 21(11), 100428. DOI:https://doi.org/10.1016/j.mcpro.2022.100428

Trypanosoma cruzi DNA Polymerase ? Is Phosphorylated In Vivo and In Vitro by Protein Kinase C (PKC) and Casein Kinase 2 (CK2)
Maldonado, E.; Rojas, D.A.; Urbina, F.; Valenzuela-Pérez, L.; Castillo, C.; Solari, A.
Cells 2022, 11, 3693. https://doi.org/10.3390/cells11223693

Ser/Thr kinase-dependent phosphorylation of the peptidoglycan hydrolase CwlA controls its export and modulates cell division in Clostridioides difficile
Garcia-Garcia T, Poncet S, Cuenot E, Douché T, Giai Gianetto Q, Peltier J, Courtin P, Chapot-Chartier M-P, Matondo M, Dupuy B, Candela T, Martin-Verstraete I.
mBio 12:e00519-21. https://doi.org/10.1128/mBio.00519-21.

Affinity-based proteomics reveals novel targets of inositol pyrophosphate (5-IP7)-dependent phosphorylation and binding in Trypanosoma cruzi replicative stages
Mantilla, BS, Kalesh, K, Brown, NW, Fiedler, D, Docampo, R.
Mol Microbiol. 2021; 115: 986–1004. https://doi.org/10.1111/mmi.14672

Identification of Phosphorylation and Other Post-Translational Modifications in the Central C4C5 Domains of Murine Cardiac Myosin Binding Protein C
Chang Yoon Doh, Katherine L. Dominic, Caitlin E. Swanberg, Nikhil Bharambe, Belinda B. Willard, Ling Li, Rajesh Ramachandran, and Julian E. Stelzer
ACS Omega, 2022, 7, 16, 14189–14202. https://doi.org/10.1021/acsomega.2c00799

Increased phosphorylation of HexM improves lysosomal uptake and potential for managing GM2 gangliosidoses
Graeme Benzie, Kristen Bouma, Taylor Battellino, Steven Cooper, Rick Hemming, Wafa Kammouni, Lin Liu, Cuong Do, Mazdak Khajehpour, Helene Perreault, Stuart Kornfeld, Barbara Triggs-Raine, Brian L. Mark
BBA Advances, 2022, 2, 100032, https://doi.org/10.1016/j.bbadva.2021.100032.

Reversible phosphorylation of cyclin T1 promotes assembly and stability of P-TEFb
Fang Huang, Trang TT Nguyen, Ignacia Echeverria, Ramachandran Rakesh, Daniele C Cary, Hana Paculova, Andrej Sali, Arthur Weiss, Boris Matija Peterlin, Koh Fujinaga
eLife 10:e68473. https://doi.org/10.7554/eLife.68473

Substrate Profiling of the Arabidopsis Ca2+-Dependent Protein Kinase Atcpk4 and its Ricinus Communis Ortholog Rccdpk1
Kilburn, Ryan and Fedosejevs, Eric T. and Mehta, Devang and Ghahremani, Mina and Thelen, Jay J. and Uhrig, Richard Glen and Snedden, Wayne A. and Plaxton, William Charles
SSRN: http://dx.doi.org/10.2139/ssrn.4238554

Serine phosphorylation regulates the P-type potassium pump KdpFABC
Marie E SweetXihui ZhangHediye Erdjument-BromageVikas DubeyHimanshu KhandeliaThomas A NeubertBjørn P PedersenDavid L Stokes
eLife, 2020, 9:e55480. https://doi.org/10.7554/eLife.55480