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. Author manuscript; available in PMC: 2011 Sep 27.
Published in final edited form as: Mol Cancer Ther. 2009 Jun 9;8(6):1505–1514. doi: 10.1158/1535-7163.MCT-08-1055

Figure 2.

Figure 2

The mAb 12A10 epitope maps to a surface on the F3 module of the Pyk2 FERM domain. SF767 cells were transfected with FLAG-tagged Pyk2 wild-type (WT) or the indicated FLAG-tagged Pyk2 variant. Pyk2 was immunoprecipitated (IP) with anti-FLAG mAb and immunoblotted (IB) with anti-phosphotyrosine mAb pY20 or mAb 12A10. Antiphosphotyrosine blot was stripped and reprobed with anti-FLAG. B, space fill model of the Pyk2 FERM F3 module highlighting the β5C-α1C surface. Substitution of residues colored blue did not affect mAb 12A10 binding, whereas substitution of residues shaded red abolished or reduced mAb 12A10 binding.