Phospho-LCP1 (Tyr28) AntibodyProduct information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Lymphocyte Signaling
Phospho-LCP1 (Tyr28) Antibody #5277
|5277S||100 µl (10 western blots)||---||In Stock||---|
|5277||carrier free and custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-LCP1 (Tyr28) Antibody detects endogenous levels of LCP1 protein only when phosphorylated on Tyr28.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr28 of human LCP1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Highly conserved and widely expressed plastin proteins comprise a subset of actin-binding proteins that include proteins that promote actin bundling. Three plastins exhibiting differential expression are found in mammals and include L-plastin, T-plastin, and I-plastin. T-plastin (plastin-3) is found in cells of most solid tissues, while I-plastin (plastin-1) is expressed specifically in the kidney, colon, and small intestine (1-3). Research studies have shown that L-plastin (plastin-2) or lymphocyte cytosolic protein 1 (LCP1) is mainly expressed in hematopoietic cells and nonhematopoietic tumors, and increased expression correlates with metastatic progression in colon cancer cell lines (4). Investigators have found that overexpression of LCP1 in premetastatic cancer cell lines induces invasion and loss of E-cadherin expression, which is characteristic of metastatic cancer cell lines (5). LCP1 becomes phosphorylated at Ser5 upon stimulation through the T cell receptor/CD3 complex in association with the CD2 cell adhesion molecule or the CD28 receptor (6). Phosphorylation at Ser5 enhances the ability of LCP1 to bind to F-actin and increases cell motility (7,8).
Phosphorylation of LCP1 on Tyr28 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery as well as other publications using MS technology (9). Phosphorylation of LCP1 at Tyr28 is seen in many leukemic cell lines (9-12).
- Lin, C.S. et al. (1993) J Biol Chem 268, 2781-92.
- Lin, C.S. et al. (1994) Mol Cell Biol 14, 2457-67.
- Delanote, V. et al. (2005) Acta Pharmacol Sin 26, 769-79.
- Otsuka, M. et al. (2001) Biochem Biophys Res Commun 289, 876-81.
- Foran, E. et al. (2006) Int J Cancer 118, 2098-104.
- Wabnitz, G.H. et al. (2007) Eur J Immunol 37, 649-62.
- Janji, B. et al. (2006) J Cell Sci 119, 1947-60.
- Klemke, M. et al. (2007) Int J Cancer 120, 2590-9.
- Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
- Rikova, K. et al. (2007) Cell 131, 1190-203.
- Gu, T.L. et al. (2007) Blood 110, 323-33.
- Walters, D.K. et al. (2006) Leuk Res 30, 1097-104.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.