p-Thr Antibody (1E11) is a mouse monoclonal IgG1 antibody that detects phosphothreonine in mouse, rat, human, and canine samples through applications such as western blotting (WB) and immunoprecipitation (IP). p-Thr monoclonal antibody (1E11) specifically recognizes phosphorylated threonine residues, which are critical for regulating various cellular processes, including signal transduction pathways. The phosphorylation of threonine residues plays a significant role in activating key mitogen-activated protein kinases (MAPKs) such as ERK and JNK, which mediate cellular responses to growth factors and stress signals. p-Thr (1E11) antibody enables researchers to investigate threonine phosphorylation dynamics and implications in cellular signaling, providing insights into mechanisms underlying various physiological and pathological conditions. p-Thr (1E11) monoclonal antibody serves as an invaluable tool for studying protein interaction networks and modifications that govern cellular behavior, advancing our understanding of cellular signaling pathways.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA
LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences
p-Thr Antibody (1E11) References:
- p13(SUC1) and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope. | Landrieu, I., et al. 2001. J Biol Chem. 276: 1434-8. PMID: 11013245
- Identification of O-phosphoserine, O-phosphothreonine and gamma-carboxyglutamic acid in the non-collagenous proteins of bovine cementum; comparison with dentin, enamel and bone. | Glimcher, MJ., et al. 1979. Calcif Tissue Int. 28: 83-6. PMID: 115557
- Catalytic subunit of protein kinase A caged at the activating phosphothreonine. | Zou, K., et al. 2002. J Am Chem Soc. 124: 8220-9. PMID: 12105899
- FHA domains as phospho-threonine binding modules in cell signaling. | Hammet, A., et al. 2003. IUBMB Life. 55: 23-7. PMID: 12716058
- AMBER force-field parameters for phosphorylated amino acids in different protonation states: phosphoserine, phosphothreonine, phosphotyrosine, and phosphohistidine. | Homeyer, N., et al. 2006. J Mol Model. 12: 281-9. PMID: 16240095
- Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. | Zhu, Y., et al. 2007. Mol Cell. 28: 899-913. PMID: 18060821
- Salmonella type III effector SpvC, a phosphothreonine lyase, contributes to reduction in inflammatory response during intestinal phase of infection. | Haneda, T., et al. 2012. Cell Microbiol. 14: 485-99. PMID: 22188134
- Synthesis of phosphopeptides containing O-phosphoserine or O-phosphothreonine. | Arendt, A., et al. 1989. Int J Pept Protein Res. 33: 468-76. PMID: 2506143
- Simultaneous formation of peptides and nucleotides from N-phosphothreonine. | Zhou, W., et al. 1996. Orig Life Evol Biosph. 26: 547-60. PMID: 9008881
- Decomposition of phosphoserine and phosphothreonine during acid hydrolysis. | Bylund, DB. and Huang, TS. 1976. Anal Biochem. 73: 477-85. PMID: 962058