Product Pathways - Tyrosine Kinase / Adaptors
Phospho-ALK (Tyr1096) (D96H9) Rabbit mAb #6962
|6962S||100 µl (10 western blots)||---||In Stock||---|
|6962||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human||Endogenous||80 (NPM-ALK) 220 (ALK)||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Mouse, Rat.
Specificity / Sensitivity
Phospho-ALK (Tyr1096) (D96H10) Rabbit mAb detects ALK only when phosphorylated at Tyr1096 (equivalent to Tyr156 of NPM-ALK).
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1096 of human ALK protein.
Anaplastic lymphoma kinase (ALK) is a tyrosine kinase receptor for pleiotrophin (PTN), a growth factor involved in embryonic brain development (1-3). In ALK-expressing cells, PTN induces phosphorylation of both ALK and the downstream effectors IRS-1, Shc, PLCγ, and PI3 kinase (1). ALK was originally discovered as a nucleophosmin (NPM)-ALK fusion protein produced by a translocation (4). Investigators have found that the NPM-ALK fusion protein is a constitutively active, oncogenic tyrosine kinase associated with anaplastic lymphoma (4). Research literature suggests that activation of PLCγ by NPM-ALK may be a crucial step for its mitogenic activity and involved in the pathogenesis of anaplastic lymphomas (5).
A distinct ALK oncogenic fusion protein involving ALK and echinoderm microtubule-associated protein like 4 (EML4) has been described in the research literature from a non-small cell lung cancer (NSCLC) cell line, with corresponding fusion transcripts present in some cases of lung adenocarcinoma. The short, amino-terminal region of the microtubule-associated protein EML4 is fused to the kinase domain of ALK (6-8).
Phosphorylation of ALK on Tyr1096 was identified at Cell Signaling Technology using PTMScan®, our LC-MS/MS platform for phosphorylation site discovery. Phosphorylation of fusion protein NPM-ALK at the Tyr1096 site was also reported by several other labs in select carcinoma cell lines and in tumors, and is shown to be important for NPM-ALK function (8,9).
- Stoica, G.E. et al. (2001) J Biol Chem 276, 16772-9.
- Iwahara, T. et al. (1997) Oncogene 14, 439-49.
- Morris, S.W. et al. (1997) Oncogene 14, 2175-88.
- Morris, S.W. et al. (1994) Science 263, 1281-4.
- Bai, R.Y. et al. (1998) Mol Cell Biol 18, 6951-61.
- Rikova, K. et al. (2007) Cell 131, 1190-203.
- Takeuchi, K. et al. (2008) Clin Cancer Res 14, 6618-24.
- Soda, M. et al. (2007) Nature 448, 561-6.
- Turner, S.D. et al. (2007) Cell Signal 19, 740-7.
- Chikamori, M. et al. (2007) Oncogene 26, 2950-4.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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