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Product last modified at: 2025-01-03T23:15:08.087Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

DAPK3/ZIPK Antibody #2928

Filter:
  • WB
Western Blotting Image 1: DAPK3/ZIPK Antibody
Western blot analysis of extracts from various cell lines using DAPK3/ZIPK Antibody.

To Purchase # 2928

Cat. # Size Qty. Price Ships
2928S 100 µl
$306

Supporting Data

REACTIVITY H M R
SENSITIVITY Endogenous
MW (kDa) 52
SOURCE Rabbit
Application Key:
  • WB-Western Blotting 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • R-Rat 

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

DAPK3/ZIPK Antibody detects endogenous levels of total DAPK3/ZIPK protein.

Species Reactivity:

Human, Mouse, Rat

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Monkey

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxyl terminus of human DAPK3/ZIPK. Antibodies were purified by protein A and peptide affinity chromatography.

Background

Death-associated protein kinase (DAPK1) is a Ca2+/calmodulin-regulated serine/threonine kinase that participates in a wide range of apoptotic signals including interferon-γ, tumor necrosis factor α, Fas, activated c-Myc, and detachment from the extracellular matrix. In addition to the kinase domain and calmodulin regulatory segment, DAPK1 also has eight ankyrin repeats, a cytoskeleton binding region, and a conserved death domain (1-3). Deletion of the calmodulin-regulatory domain generates a constitutively active mutant kinase. Ectopic expression of wild-type DAPK1 induced cell death in HeLa cells. Conversely, expression of a catalytically inactive mutant protected cells from interferon-γ-induced cell death (4). The catalytic domain of DAPK1 has very high sequence similarity to vertebrate myosin light chain kinase (MLCK) and a RXX(S/T)X motif derived from myosin light chain protein was shown to be phosphorylated in vitro by DAPK1 (5).
The DAPK family consists of several kinases including DAPK, DAPK2/DRP-1 (6), and DAPK3/ZIPK/DLK (7-9) with homology in their catalytic domain. Overexpression of DAPK3/ZIPK, but not a catalytically inactive mutant, can induce apoptosis (7). DAPK3 was also identified as a myosin light chain kinase, demonstrating ability to phosphorylate the regulatory light chain of myosin II in a Ca2+/calmodulin-independent manner (8). In addition to an amino-terminal kinase domain, DAPK3 contains a carboxy-terminal leucine zipper domain that mediates interaction with leucine zipper transcription factors such as ATF4 (7). DAPK3 is predominantly localized to the nucleus and has been found in PML oncogenic domains (PODs) associated with DAXX and PAR-4, and can phosphorylate PAR-4 in vitro (10,11). In addition, DAPK3 can phosphorylate STAT3 at Ser727 to enhance its transcriptional activity (12).
For Research Use Only. Not For Use In Diagnostic Procedures.
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