Rabbit DAP Kinase 3, (Death-associated protein kinase 3 (Internal Epitope) Polyclonal Antibody | anti-DAPK3 antibody

DAP Kinase 3 (IN), (Death-associated protein kinase 3 (Internal Epitope)

Cat. Num. AAA395661

• Gene Names: DAPK3; ZIP; ZIPK
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot
• Purity: Antigen Immunoaffiinity Purification
• Synonyms: DAP Kinase 3; (Death-associated protein kinase 3 (Internal Epitope); Polyclonal Antibody; DAP Kinase 3 (IN); ZIP kinase; Internal; DAPK3; anti-DAPK3 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Antigen Immunoaffiinity Purification
• Form/Format: Provided in phosphate buffered saline solution containing 0.02% sodium azide as a preservative
• Sequence Length: 454

• Applicable Applications for anti-DAPK3 antibody: Western Blot (WB)
• Immunogen: Antibody raised against a synthetic protein corresponding to amino acids 279 to 298 of the human ZIP kinase protein.
• Positive Control: Jurkat and HeLa whole cell lysates
• Preparation and Storage: Product should be stored at -20 degree C. Aliquot to avoid freeze/thaw cycles

Western Blot/Blotting

(Western blot analysis)

Related Product Information for anti-DAPK3 antibody

Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. A novel serine/threonine kinase that mediates apoptosis was recently identified and designated ZIP kinase1. ZIP kinase contains an N-terminal kinase domain and a C-terminal leucine zipper structure and binds to ATF4 that is a member of ATF/CREB family. ZIP kinase has high sequence homology to DAP kinase (death-associated protein kinase), which is a mediator of apoptosis induced by gamma interferon. Overexpression of ZIP kinase induces apoptosis. ZIP and DAP kinases represent a novel kinase family, which mediates apoptosis through their catalytic activities. The messenger RNA was ubiquitously expressed in various tissues1.

Product Categories/Family for anti-DAPK3 antibody

Polyclonal Antibody; Apoptosis Regulating Kinases

NCBI and Uniprot Product Information

• NCBI GI #: 4557511
• NCBI GeneID: 1613
• NCBI Accession #: NP_001339.1
• NCBI GenBank Nucleotide #: NM_001348.1
• UniProt Accession #: O43293; Q05JY4; A0AVN4; B3KQE2
• Molecular Weight: 50
• NCBI Official Full Name: death-associated protein kinase 3
• NCBI Official Synonym Full Names: death-associated protein kinase 3
• NCBI Official Symbol: DAPK3
• NCBI Official Synonym Symbols: ZIP; ZIPK
• NCBI Protein Information: death-associated protein kinase 3; dlk; ZIP-kinase; DAP kinase 3; MYPT1 kinase; DAP-like kinase; ZIP kinase isoform; zipper-interacting protein kinase
• UniProt Protein Name: Death-associated protein kinase 3
• Protein Family: Death-associated protein kinase
• UniProt Gene Name: DAPK3
• UniProt Synonym Gene Names: ZIPK; DAP kinase 3; Dlk; ZIP-kinase
• UniProt Entry Name: DAPK3_HUMAN

NCBI Description

Death-associated protein kinase 3 (DAPK3) induces morphological changes in apoptosis when overexpressed in mammalian cells. These results suggest that DAPK3 may play a role in the induction of apoptosis. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation, actin cytoskeleton reorganization, cell motility, smooth muscle contraction, and mitosis, particularly cytokinesis. Regulates both type I apoptotic and type II autophagic cell deaths signal, 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. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A, and the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca2+ and promote a contractile state. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates STAT3 and enhances its transcriptional activity. Positively regulates the canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Can disrupt the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, its association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Ref.2 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.17 Ref.20 Ref.21 Ref.23 Ref.24Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Ref.2 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.17 Ref.20 Ref.21 Ref.23 Ref.24

Catalytic activity: ATP + a protein = ADP + a phosphoprotein. Ref.2

Cofactor: Magnesium. Ref.2

Enzyme regulation: Inhibited by pyridone 6 (K00225), a potent, ATP-competitive inhibitor. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Oligomerization is required for full enzymatic activity. Ref.11 Ref.14 Ref.17

Subunit structure: Monomer and homotrimer. Can also exist as homodimer or form heterodimers with ATF4. Homodimerization is required for activation segment autophosphorylation Both interactions require an intact leucine zipper domain and oligomerization is required for full enzymatic activity. Also binds to DAXX and PAWR, possibly in a ternary complex which plays a role in caspase activation. According to Ref.18, does not interact with PARW. Interacts with AATF, CDC5L, UBE2D1, UBE2D2 AND UBE2D3. Interacts with AR and this interaction is enhanced by AATF. Interacts (via leucine zipper) with TCP10L (via leucine zipper). Interacts (via kinase domain) with DAPK1 (via kinase domain). Interacts with STAT3, NLK and TCF7L2. Isoform 1 and isoform 2 can interact with myosin and PPP1R12A. Ref.5 Ref.7 Ref.9 Ref.11 Ref.12 Ref.13 Ref.18 Ref.20 Ref.21 Ref.23 Ref.24

Subcellular location: Nucleus. Cytoplasm Ref.5 Ref.6 Ref.8 Ref.9 Ref.13 Ref.18 Ref.20 Ref.22. Nucleus › PML body. Chromosome › centromere. Cytoplasm › cytoskeleton › centrosome. Note: The phosphorylated form is anchored in the cytoplasm and/or prevented from being shuttled to the nucleus, whereas nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation at Thr-299 promotes cytoplasmic localization. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments. Localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs). Associated: with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis. Ref.5 Ref.6 Ref.8 Ref.9 Ref.13 Ref.18 Ref.20 Ref.22Isoform 2: Nucleus. Cytoplasm Ref.5 Ref.6 Ref.8 Ref.9 Ref.13 Ref.18 Ref.20 Ref.22.

Tissue specificity: Isoform 2 is expressed in the bladder smooth muscle. Ref.5

Post-translational modification: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus.The phosphorylation status is critical for: its intracellular localization, ability to oligomerize and its activity. The phosphorylated form is anchored in the cytoplasm and/or prevented from being shuttled to the nucleus, whereas nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation shifts the equilibrium towards the monomeric form. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Phosphorylation at Thr-299 promotes cytoplasmic localization. A species-specific loss of a key phosphorylation site in murine DAPK3 seems to direct it to the nucleus, while the presence of the Thr-299 site in human DAPK3 correlates with cytoplasmic localization. Both isoform 1 and isoform 2 can undergo autophosphorylation. Ref.5 Ref.9 Ref.11 Ref.14 Ref.16 Ref.17 Ref.22

Miscellaneous: The murine DAPK3 protein differs from the human ortholog, losing an important phosphorylation site and displaying distinct altered cellular localization. The murine protein localizes only to the nucleus while the human protein shows both nuclear and cytoplasmic localization. A different protein interaction capacity, with an important protein partner in the apoptosis pathway (PAWR), evolved in the murine system to maintain the basic membrane blebbing function in the apoptosis pathway.

Sequence similarities: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily.Contains 1 protein kinase domain.

Biophysicochemical propertiesKinetic parameters:KM=12 µM for myosin (isoform 2) Ref.5KM=6.2 µM for myosin (isoform 1)KM=73 µM for MYL12B (isoform 2)KM=10.4 µM for MYL12B (isoform 1)Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2)Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1)Vmax=1.3 µmol/min/mg enzyme toward MYL12B (isoform 2)Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1)