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Western blot analysis of Tyk2 (pY1054/pY1055) in human Burkitt's lymphoma. Lysates from control (left panel) and IFN-α-activated (right panel) Daudi cells were probed with purified mouse anti-Tyk2 (pY1054/pY1055) monoclonal antibody) at concentrations of 4, 2, and 1 µg/ml (Lanes 1, 2, and 3, respectively). Tyk2 (pY1054/pY1055) is identified as a band of 135 kDa in the treated cells.
BD Pharmingen™ Purified Mouse anti-Tyk2 (pY1054/pY1055)
Regulatory Status Legend
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Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
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Tyk2 is a widely expressed protein tyrosine kinase (PTK) of 1187 amino acids (135 kDa). The N-terminal kinase-related domain of Tyk2 shows 54% identity to the kinase-related domain of the JAK1 kinase. Surprisingly, the catalytic region of JAK1 shares more sequence identity to Tyk2 than it does with JAK2 kinase. The similarity of structure between Tyk2 and JAK1 suggests that both may be involved in related phosphorylation cascades. Tyk2 plays a critical role in the interferon (IFN)-α/β response while JAK1 shows involvement in both the IFN- α/β and IFN-γ signal transduction pathways. JAK2, however, appears to be required only in the IFN-γ response. It has been suggested that a portion of the large extracatalytic domain of Tyk2 could interact with components of the IFN α/β receptor.
The I114-617 monoclonal antibody recognizes the phosphorylated Y1054 and Y1055 in the tyrosine kinase domain of Tyk2.
Development References (1)
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Gauzzi MC, Velazquez L, McKendry R, Mogensen KE, Fellous M, Pellegrini S. Interferon-alpha-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. J Biol Chem. 1996; 271(34):20494-20500. (Biology).
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