p-Thr Antibody (14B3) 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 (14B3) specifically recognizes phosphorylated threonine residues, which are critical for regulating various cellular processes, including signal transduction pathways. Phosphorylation of threonine plays a pivotal 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 (14B3) 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 (14B3) 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.
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p-Thr Antibody (14B3) References:
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- SpvC is a Salmonella effector with phosphothreonine lyase activity on host mitogen-activated protein kinases. | Mazurkiewicz, P., et al. 2008. Mol Microbiol. 67: 1371-83. PMID: 18284579
- Detection and assignment of phosphoserine and phosphothreonine residues by (13)C- (31)P spin-echo difference NMR spectroscopy. | McIntosh, LP., et al. 2009. J Biomol NMR. 43: 31-7. PMID: 19002654
- Structural and functional analysis of phosphothreonine-dependent FHA domain interactions. | Pennell, S., et al. 2010. Structure. 18: 1587-95. PMID: 21134638
- Computational investigation of the enzymatic mechanisms of phosphothreonine lyase. | Pei, Q., et al. 2011. Biophys Chem. 157: 16-23. PMID: 21558045
- OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order. | Brister, MA., et al. 2014. J Am Chem Soc. 136: 3803-16. PMID: 24559475
- The pellino e3 ubiquitin ligases recognize specific phosphothreonine motifs and have distinct substrate specificities. | Huoh, YS. and Ferguson, KM. 2014. Biochemistry. 53: 4946-55. PMID: 25027698
- Michael addition of dehydroalanine-containing MAPK peptides to catalytic lysine inhibits the activity of phosphothreonine lyase. | Zhang, Y., et al. 2015. FEBS Lett. 589: 3648-53. PMID: 26519561
- EYA1's Conformation Specificity in Dephosphorylating Phosphothreonine in Myc and Its Activity on Myc Stabilization in Breast Cancer. | Li, J., et al. 2017. Mol Cell Biol. 37: PMID: 27795300
- Threonine eliminylation by bacterial phosphothreonine lyases rapidly causes cross-linking of mitogen-activated protein kinase (MAPK) in live cells. | Meijer, BM., et al. 2017. J Biol Chem. 292: 7784-7794. PMID: 28325837