Anti-phospho-DAP-Kinase (pSer308) antibody, Mouse monoclonal

Uses

Anti-phospho-DAP-Kinase (pSer308) antibody, Mouse monoclonal has been used in:

• western blot assay
• immunocytochemistry
• enzyme linked immunosorbent assay (ELISA)
• immunoprecipitation

General Description

Monoclonal Anti-phospho DAP-Kinase (pSer308) (mouse IgG1 isotype) is derived from the DKPS308 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a phosphopeptide of human DAP-kinase, conjugated to KLH. Death Associated Protein Kinase (DAPK) is characterized with a multidomain structure including subdomain typical of serine/threonine kinases, a Ca²⁺/calmodulin regulatory domain, eight ankyrin repeats followed by two P-loop motifs and a typical death domain module. In addition, it also contains two auto-inhibitory domains, one of them Ca²⁺/calmodulin dependent. In the absence of this latter domain, DAPK is constitutively active.

Biochem/physiol Actions

Death Associated Protein Kinase (DAPK) plays crucial role in programmed cell death as well as in autophagy. DAPK activity is regulated by phosphorylation. Autophosphorylation at Ser308 on the calmodulin regulatory domain negatively regulate DAPK activity. This autophosphorylation, which occurs in cells at the basal state, lowers the affinity of DAPK for calmodulin and thus the kinase is inactive. Under some apoptotic conditions DAPK undergoes dephosphorylation. Consequently, it binds to calmodulin with higher affinity, becomes activated, phosphorylates its downstream substrate proteins, and mediates apoptosis. Monoclonal anti-phospho-DAP-kinase (pSer308) antibody can be used to study the mechanism of DAPK activation in apoptosis. It can also be used in microarray.