质量标准：【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).
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.
B. Immunohistochemical staining of paraffin-embedded
human liver carcinoma using anti-DAPK2 RabMAb (cat. #2009-1).
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