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REACTIVITY SENSITIVITY MW (kDa) Isotype
H Endogenous 80 (NPM-ALK) 220 (ALK) Rabbit IgG

Western blot analysis of extracts from SUP-M2 cells, untreated or treated with calf intestinal phosphatase (CIP), using Phospho-ALK (Tyr1096) (D96H10) Rabbit mAb (upper) and ALK (C26G7) Rabbit mAb #3333 (lower).

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Product Usage Information

Application Dilutions
Western Blotting 1:1000
Immunoprecipitation 1:50

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Phospho-ALK (Tyr1096) (D96H10) Rabbit mAb detects ALK only when phosphorylated at Tyr1096 (equivalent to Tyr156 of NPM-ALK).


Species Reactivity: Human
Species predicted to react based on 100% sequence homology: Mouse, Rat

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).


1.  Stoica, G.E. et al. (2001) J Biol Chem 276, 16772-9.

2.  Iwahara, T. et al. (1997) Oncogene 14, 439-49.

3.  Morris, S.W. et al. (1997) Oncogene 14, 2175-88.

4.  Morris, S.W. et al. (1994) Science 263, 1281-4.

5.  Bai, R.Y. et al. (1998) Mol Cell Biol 18, 6951-61.

6.  Takeuchi, K. et al. (2008) Clin Cancer Res 14, 6618-24.

7.  Soda, M. et al. (2007) Nature 448, 561-6.

8.  Rikova, K. et al. (2007) Cell 131, 1190-203.

9.  Turner, S.D. et al. (2007) Cell Signal 19, 740-7.

10.  Chikamori, M. et al. (2007) Oncogene 26, 2950-4.


Entrez-Gene Id 238
Swiss-Prot Acc. Q9UM73


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