Dapk3 blocking peptide

Mouse Dapk3 Antibody (Center) Blocking Peptide

• Gene Names: Dapk3; dlk; ZIPK
• Synonyms: Dapk3; Mouse Dapk3 Antibody (Center) Blocking Peptide; Death-associated protein kinase 3; DAP kinase 3; DAP-like kinase; Dlk; MYPT1 kinase; ZIP-kinase; Zipk; Dapk3 blocking peptide

• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 448

• Cellular Location: Nucleus. Nucleus, PML body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere. Cytoplasm. Note: Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments. Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis (By similarity)
• Tissue Location: Highly expressed in heart, brain, lung, skeletal muscle, kidney and testis. Lower levels in liver and spleen.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for Dapk3 blocking peptide

Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase- dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its transcriptional activity. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis (By similarity). Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition.

NCBI and Uniprot Product Information

• NCBI GI #: 38604695
• NCBI GeneID: 13144
• UniProt Accession #: O54784
• Molecular Weight: 51,422 Da
• 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: dlk; ZIPK
• NCBI Protein Information: death-associated protein kinase 3
• 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
• UniProt Entry Name: DAPK3_MOUSE

Uniprot Description

DAPK3: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, 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 Ca(2+) 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. 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 PubMed:17953487, 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. Isoform 2 is expressed in the bladder smooth muscle. 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. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Protein kinase, Ser/Thr (non-receptor); Protein kinase, CAMK; Kinase, protein; Tumor suppressor; EC 2.7.11.1; CAMK group; DAPK family

Cellular Component: actin filament; cytoplasm; lipid raft; nucleus; PML body

Molecular Function: ATP binding; identical protein binding; kinase activity; leucine zipper domain binding; protein binding; protein C-terminus binding; protein homodimerization activity; protein serine/threonine kinase activity; Rho GTPase binding

Biological Process: apoptosis; negative regulation of translation; positive regulation of apoptosis; positive regulation of cell migration; protein amino acid autophosphorylation; protein amino acid phosphorylation; regulation of cell shape; regulation of focal adhesion formation; regulation of mitotic cell cycle; regulation of myosin II filament assembly or disassembly