Phospho-ALK (Tyr1507) (D6F1V) Rabbit mAb #14678
- WB
- IP
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 80 (NPM-ALK), 220 (ALK) |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunofluorescence (Immunocytochemistry) | 1:400 |
| Flow Cytometry (Fixed/Permeabilized) | 1:200 |
Storage
Protocol
Specificity / Sensitivity
Phospho-ALK (Tyr1507) (D6F1V) Rabbit mAb recognizes endogenous levels of ALK protein only when phosphorylated at Tyr1507 (equivalent to Tyr567 of NPM-ALK).
Species Reactivity:
Human
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
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 Tyr1507 of human ALK protein.
Background
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 Tyr1507 was identified at Cell Signaling Technology using PhosphoScan®, an LC-MS/MS platform used for phosphorylation site discovery (6). Phosphorylation of ALK at Tyr1507 (Tyr567 in NPM-ALK) has been shown to be important for interaction with the adaptor proteins Shc, FRS2-α, and FRS2-β (9,10).
- 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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