D4941
Anti-phospho-DAP-Kinase (pSer308) antibody, Mouse monoclonal
clone DKPS308, purified from hybridoma cell culture
Synonym(s):
Anti-DAPK, Anti-ROCO3
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About This Item
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
DKPS308, monoclonal
form
buffered aqueous solution
mol wt
antigen ~160 kDa
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using 293T (human embryonal kidney) cells transfected with DAP-kinase expression vector.
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
phosphorylation (pSer308)
Gene Information
human ... DAPK1(1612)
Related Categories
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.
Immunogen
Phosphopeptide corresponding to amino acids 303-312 (pSer308) of human DAP-kinase, conjugated to KLH.
Application
Anti-phospho-DAP-Kinase (pSer308) antibody, Mouse monoclonal has been used in:
- western blot assay
- immunocytochemistry
- enzyme linked immunosorbent assay (ELISA)
- immunoprecipitation
Monoclonal anti-phospho-DAP-kinase (pSer308) antibody can be used in indirect ELISA, immunoblotting and immunoprecipitation. It can also be used in western blotting.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Certificates of Analysis (COA)
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Xiao-Hui Li et al.
Neural regeneration research, 18(8), 1795-1801 (2023-02-09)
We previously showed that death-associated protein kinase 1 (DAPK1) expression is increased in hippocampal tissue in a mouse model of major depressive disorde and is related to cognitive dysfunction in Alzheimer's disease. In addition, depression is a risk factor for
The role of DAPK-BimEL pathway in neuronal death induced by oxygen-glucose deprivation
He C, et al.
Neuroscience, 258, 254-254 (2014)
The Pro-apoptotic Function of Death-associated Protein Kinase Is Controlled by a Unique Inhibitory Autophosphorylation-based Mechanism
Shohat G, et al.
Test, 276, 47460-47467 (2001)
Song Liu et al.
Frontiers in neuroscience, 15, 525615-525615 (2021-03-12)
Excitatory toxicity due to excessive glutamate release is considered the core pathophysiological mechanism of cerebral ischemia. It is primarily mediated by N-methyl-D-aspartate receptors (NMDARs) on neuronal membranes. Our previous studies have found that icaritin (ICT) exhibits neuroprotective effects against cerebral
A functional genetic screen identifies regions at the C-terminal tail and death-domain of death-associated protein kinase that are critical for its proapoptotic activity
Raveh T, et al.
Proceedings of the National Academy of Sciences of the USA, 97, 1572-1577 (2000)
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