Phospho-DAPK3 (T265) Polyclonal Antibody, 100µg, (ATB-P0548)

Description

Background:

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]

Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. 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; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca²⁺ and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. 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. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor.

Product datasheet:

Overview
Product Description	Phospho-DAPK3 (T265) Polyclonal Antibody, 100µg, (ATB-P0548)
Image
Species Reactivities	Human,Mouse,Rat
Immunogen	Synthesized peptide derived from human DAPK3 around the phosphorylation site of T265.
Properties
Form	Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions	-20°C/1 year
Clonality	Polyclonal

References:

1. ZIPK is critical for the motility and contractility of VSMCs through the regulation of nonmuscle myosin II isoforms. Komatsu S, et al. Am J Physiol Heart Circ Physiol, 2014 May. PMID 24633547 Free PMC Article
2. Cancer-associated loss-of-function mutations implicate DAPK3 as a tumor-suppressing kinase. Brognard J, et al. Cancer Res, 2011 Apr 15. PMID 21487036 Free PMC Article
3. Link of Dlk/ZIP kinase to cell apoptosis and tumor suppression. Wu Y, et al. Biochem Biophys Res Commun, 2010 Feb 19. PMID 20085750
4. Downregulation of ZIP kinase is associated with tumor invasion, metastasis and poor prognosis in gastric cancer. Bi J, et al. Int J Cancer, 2009 Apr 1. PMID 19117059
5. ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells. Murata-Hori M, et al. FEBS Lett, 1999 May 14. PMID 10356987
6. ZIP kinase, a novel serine/threonine kinase which mediates apoptosis.
   Kawai T., Matsumoto M., Takeda K., Sanjo H., Akira S.
   Mol. Cell. Biol. 18:1642-1651(1998) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
7. ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells.
   Murata-Hori M., Suizu F., Iwasaki T., Kikuchi A., Hosoya H.
   FEBS Lett. 451:81-84(1999) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR. Tissue: Cervix carcinoma.
8. Complete sequencing and characterization of 21,243 full-length human cDNAs.
   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
   , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
   Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC]

   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

9. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
10. Novel ZIP kinase isoform lacks leucine zipper.
    Takamoto N., Komatsu S., Komaba S., Niiro N., Ikebe M.
    Arch. Biochem. Biophys. 456:194-203(2006) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-454 (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION IN PHOSPHORYLATION OF MYOSIN; PPP1R12A AND MYL12B, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PPP1R12A AND MYOSIN, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY. Tissue: Urinary bladder.