【产品介绍】Protein kinase termed death-associated protein kinase 2 (DAPK2) dependant on calcium/ calmodulin (Ca2+/CaM) contains an N-terminal protein kinase domain followed by a conserved CaM-binding domain with significant homologies to those of DAP kinase, a protein kinase involved in apoptosis. Overexpression of DAPK2 significantly induced the m o r phological changes characteristic of apoptosis. Results indicate that DAPK2 is an additional member of DAP kinase family involved in apoptotic signaling (1). The region of homology spans the catalytic domain a n d the CaM-regulat o r y region, whereas the remaining C-terminal part of the protein differs completely from DAP kinase a n d displays no homology to any known protein. The catalytic domain is also homologous to the recently identified ZIP kinase a n d to a lesser extent to the catalytic domains of DRAK1 a n d -2 (2). DAPK2 has a novel regulat o r y mechanism that controls its pro-apoptotic functions. It comprises a single autophosph o r ylation event mapped to Ser308 within the CaM regulat o r y domain. A negative charge at this site reduces both the binding to CaM a n d the f o r mation of DRP-1 homodimers (3). DAPK2 (N-term),Rabbit Monoclonal IgG WB: 1:2000 IHC: 1:50 100 Flow Cytometry: 1:15 A. Western blot analysis on rat spleen lysate using anti-DAPK2 RabMAb (cat. # 2009-1), dilution 1:2000. DAPK2 (N-term),Rabbit Monoclonal IgG B. Immunohistochemical staining of paraffin-embedded human liver carcinoma using anti-DAPK2 RabMAb (cat. #2009-1). |