Phospho-TNK1 (Tyr277) (D46E7)

5638:

Western Blotting

Phospho-TNK1 (Tyr277) (D46E7) Rabbit mAb detects endogenous levels of TNK1 protein only when the amplified gene product is phosphorylated at Tyr277.

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr277 of human TNK1 protein.

Western Blotting

Western blot analysis of extracts from L-540 cells, untreated or pre-incubated with either a site-specific phosphorylated peptide to block the signal or a site-specific non-phosphorylated peptide, using Phospho-TNK1 (Tyr277) (D46E7) Rabbit mAb. L-540 cells express a 58 kDa TNK1-C17orf61 fusion protein containing 466 amino acids from the amino terminus of TNK1 [Gu, T.L. et al. (2010) Leukemia ].

Tyrosine kinase non-receptor 1 (TNK1) is related to the Ack1 (TNK2) non-receptor kinase that binds cdc42 and inhibits GTPase activity of this cell cycle regulator. TNK1 is broadly expressed in embryogenic tissues and leukemia cell lines, but is restricted to select adult tissues (1). TNK1 is a putative 72 kDa protein comprised of an N-terminal kinase domain, a central SH3 domain and a proline-rich tail. Interaction with PLCγ in vitro indicates a possible role in phospholipid signal transduction pathways (2). Though the exact mechanism is currently unclear, active TNK1 may play a role in regulating cell death by preventing TNF-α-induced NF-κB transactivation (3).

Phosphorylation of TNK1 on Tyr277 was identified at Cell Signaling Technology (CST) using PhosphoScan^® , CST's LC-MS/MS platform for phosphorylation site discovery (4) and also reported independently in another publication using MS technology (5). Phosphorylation of TNK1 at Tyr277 was observed in select carcinoma cell lines and in tumors. A constitutively active, 58 kDa truncated TNK1 kinase resulting from fusion between the TNK1 and C17orf61 genes is seen in some cells (5). For additional information, visit PhosphoSitePlus™, CST's modification site knowledgebase, at www.phosphosite.org.

1. Hoehn, G.T. et al. (1996) Oncogene 12, 903-13.
2. Felschow, D.M. et al. (2000) Biochem Biophys Res Commun 273, 294-301.
3. Azoitei, N. et al. (2007) Oncogene 26, 6536-45.
4. Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
5. Gu, T.L. et al. (2010) Leukemia 24, 861-5.

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