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48-602MAG
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07-1229
Sigma-AldrichAnti-DAPK2 Antibody
Detect DAPK2 using this Anti-DAPK2 Antibody validated for use in WB, IH(P).
More>>Detect DAPK2 using this Anti-DAPK2 Antibody validated for use in WB, IH(P). Less<<
Anti-DAPK2 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Death Associated Protein Kinase (DAPK) is a Ca2+/Calmodulin-dependent, cytoskeletal associated protein kinase whose expression is implicated in the sensitivity of cells to apoptotic effects of TNFα and Interferon-γ. Deletion of the Calmodulin-binding domain results in a constitutively active mutant with a more potent cytotoxic effect. In contrast, the catalytically inactive mutant exerts a dominant negative effect, reducing cytotoxicity and protecting cells from Interferon-γ induced cell death. DAPK expression is frequently lost in human carcinomas and B-cell leukemia, and lower levels of expression correlate with high rates of metastasis.
References
Product Information
Format
Affinity Purified
Control
C2C12 cell lysate
Presentation
Purified rabbit polyclonal IgG in buffer containing PBS and 0.02% sodium azide.
Detect DAPK2 using this Anti-DAPK2 Antibody validated for use in WB, IH(P).
Key Applications
Western Blotting
Immunohistochemistry (Paraffin)
Application Notes
Immunohistochemisty (paraffin): DAPK2 representative staining pattern/morphology in apoptotic bodies in colon cancer. Tissue was pretreated with citrate pH 6, antigen retrieval. A previous lot of this antibody was diluted to 1:100, using IHC-Select® Detection with HRP-DAB.
Western Blot: A previous lot of this antibody was tested on multiple lysates. See datasheet.
Biological Information
Immunogen
Peptide corresponding to aa 356-370 (ARRKALHPRRRSSTS) of human DAPK2, which is identical to the sequence of mouse origin.
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
Detects a 42 kDa band by western blot, corresponding to DAPK2. Does not cross-react with DAPK1.
This gene encodes a protein that belongs to the serine/threonine protein kinase family. This protein contains a N-terminal protein kinase domain followed by a conserved calmodulin-binding domain with significant similarity to that of death-associated protein kinase 1 (DAPK1), a positive regulator of programmed cell death. Overexpression of this gene was shown to induce cell apoptosis. It uses multiple polyadenylation sites.
FUNCTION: SwissProt: Q9UIK4 # Calcium/calmodulin-dependent serine/threonine kinase which acts as a positive regulator of apoptosis. COFACTOR: Magnesium. SIZE: 370 amino acids; 42898 Da SUBUNIT: Homodimer. Homodimerization is required for apoptotic function and is inhibited by autophosphorylation at Ser-318. SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Ubiquitously expressed in all tissue types examined. High levels in heart, lung and skeletal muscle. SIMILARITY: SwissProt: Q9UIK4 ## Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily. & Contains 1 protein kinase domain. ...
Molecular Weight
Detects a 42 kDa band by western blot.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Routinely evaluated by Western Blot on C2C12 lysates.
Western Blot Analysis: 1:500-1,1000 dilution of this lot detected DAPK2 on 10 μg of C2C12 lysates.
Usage Statement
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.
Storage and Shipping Information
Storage Conditions
Stable for 6 months at 2-8° C from date of receiept.
PIAS3 activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status. Dabir, S; Kluge, A; McColl, K; Liu, Y; Lam, M; Halmos, B; Wildey, G; Dowlati, A International journal of cancer. Journal international du cancer
134
1045-54
2014
Protein inhibitor of activated signal transducer and activator of transcription 3 (STAT3) (PIAS3) is an endogenous inhibitor of STAT3 that negatively regulates STAT3 transcriptional activity and cell growth and demonstrates limited expression in the majority of human squamous cell carcinomas of the lung. In this study, we sought to determine whether PIAS3 inhibits cell growth in non-small cell lung cancer cell lines by inducing apoptosis. Our results demonstrate that overexpression of PIAS3 promotes mitochondrial depolarization, leading to cytochrome c release, caspase 9 and 3 activation and poly (ADP-ribose) polymerase cleavage. This intrinsic pathway activation was associated with decreased Bcl-xL expression and increased Noxa expression and was independent of p53 status. Furthermore, PIAS3 inhibition of STAT3 activity was also p53 independent. Microarray experiments were performed to discover STAT3-independent mediators of PIAS3-induced apoptosis by comparing the apoptotic gene expression signature induced by PIAS3 overexpression with that induced by STAT3 siRNA. The results showed that a subset of apoptotic genes was uniquely expressed only after PIAS3 expression. Thus, PIAS3 may represent a promising lung cancer therapeutic target because of its p53-independent efficacy and its potential to synergize with Bcl-2 targeted inhibitors.
Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis. Inbal, B, et al. Mol. Cell. Biol., 20: 1044-54 (2000)
1999
Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity. Kawai, T, et al. Oncogene, 18: 3471-80 (1999)
1998
We have identified and characterized a new calcium/calmodulin (Ca2+/CaM) dependent protein kinase termed death-associated protein kinase 2 (DAPK2) that 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. DAPK2 mRNA is expressed abundantly in heart, lung and skeletal muscle. The mapping results indicated that DAPK2 is located in the central region of mouse chromosome 9. In vitro kinase assay revealed that DAPK2 is autophosphorylated and phosphorylates myosin light chain (MLC) as an exogenous substrate. DAPK2 binds directly to CaM and is activated in a Ca2+/CaM-dependent manner. A constitutively active DAPK2 mutant is generated by removal of the CaM-binding domain (deltaCaM). Treatment of agonists that elevate intracellular Ca2+-concentration led to the activation of DAPK2 and transfection studies revealed that DAPK2 is localized in the cytoplasm. Overexpression of DAPK2, but not the kinase negative mutant, significantly induced the morphological changes characteristic of apoptosis. These results indicate that DAPK2 is an additional member of DAP kinase family involved in apoptotic signaling.
