Cell Signaling Technology

Product Pathways - Lymphocyte Signaling

Phospho-LCP1 (Tyr28) Antibody #5277

Applications Reactivity Sensitivity MW (kDa) Source
W H Endogenous 70 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from MOLT-15 and MV-4-11 cells, untreated or treated with λ-phosphatase, using Phospho-LCP1 (Tyr28) Antibody (upper) and LCP1 Antibody #5350 (lower).

Background

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).

  1. Lin, C.S. et al. (1993) J Biol Chem 268, 2781-92.
  2. Lin, C.S. et al. (1994) Mol Cell Biol 14, 2457-67.
  3. Delanote, V. et al. (2005) Acta Pharmacol Sin 26, 769-79.
  4. Otsuka, M. et al. (2001) Biochem Biophys Res Commun 289, 876-81.
  5. Foran, E. et al. (2006) Int J Cancer 118, 2098-104.
  6. Wabnitz, G.H. et al. (2007) Eur J Immunol 37, 649-62.
  7. Janji, B. et al. (2006) J Cell Sci 119, 1947-60.
  8. Klemke, M. et al. (2007) Int J Cancer 120, 2590-9.
  9. Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
  10. Rikova, K. et al. (2007) Cell 131, 1190-203.
  11. Gu, T.L. et al. (2007) Blood 110, 323-33.
  12. Walters, D.K. et al. (2006) Leuk Res 30, 1097-104.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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