|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||42898 Da|
|Other Names||Death-associated protein kinase 2, DAP kinase 2, DAP-kinase-related protein 1, DRP-1, DAPK2|
|Target/Specificity||A synthetic peptide corresponding to residues on the N-terminus of human DAPK2 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||DAPK2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (PubMed:17347302). Regulates granulocytic motility by controlling cell spreading and polarization (PubMed:24163421).|
|Cellular Location||Cytoplasm. Cytoplasmic vesicle, autophagosome lumen|
|Tissue Location||Expressed in neutrophils and eosinophils (PubMed:24163421). Isoform 2 is expressed in embryonic stem cells (at protein level). Isoform 1 is ubiquitously expressed in all tissue types examined with high levels in heart, lung and skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
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 morphological 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 and the CaM-regulatory region, whereas the remaining C-terminal part of the protein differs completely from DAP kinase and displays no homology to any known protein. The catalytic domain is also homologous to the recently identified ZIP kinase and to a lesser extent to the catalytic domains of DRAK1 and -2 (2). DAPK2 has a novel regulatory mechanism that controls its pro-apoptotic functions. It comprises a single autophosphorylation event mapped to Ser308 within the CaM regulatory domain. A negative charge at this site reduces both the binding to CaM and the formation of DRP-1 homodimers (3).
1. Kawai T, et al. Oncogene 18(23):3471-80, 1999.
2. Inbal B, et al. Mol Cell Biol 20(3):1044-54, 2000.
3. Shani G, et al. EMBO J 20(5):1099-113, 2001.
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