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Mouse Anti-DAPK3 Recombinant Antibody (2H1D11) (CBMAB-Z0095-LY)

The product is antibody recognizes DAPK3. The antibody 2H1D11 immunoassay techniques such as: WB, IHC, FC.
See all DAPK3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
2H1D11
Antibody Isotype
IgG1
Application
WB, IHC, FC

Basic Information

Immunogen
Purified recombinant fragment of human DAPK3 (AA: 28-161) expressed in E. Coli.
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
Purified antibody in PBS with 0.05% sodium azide.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
DAPK3
Introduction
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.
Entrez Gene ID
1613
UniProt ID
O43293
Alternative Names
ZIP; ZIPK
Function
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.
Biological Process
Apoptotic process Source: UniProtKB
Apoptotic signaling pathway Source: Ensembl
Cellular response to interferon-gamma Source: UniProtKB
Chromatin organization Source: UniProtKB-KW
Intracellular signal transduction Source: UniProtKB
Negative regulation of translation Source: UniProtKB
Neuron differentiation Source: Ensembl
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of canonical Wnt signaling pathway Source: UniProtKB
Positive regulation of cell migration Source: Ensembl
Positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of actin cytoskeleton reorganization Source: UniProtKB
Regulation of apoptotic process Source: UniProtKB
Regulation of autophagy Source: UniProtKB
Regulation of cell motility Source: UniProtKB
Regulation of cell shape Source: Ensembl
Regulation of focal adhesion assembly Source: UniProtKB
Regulation of mitotic cell cycle Source: UniProtKB
Regulation of mitotic nuclear division Source: UniProtKB
Regulation of myosin II filament organization Source: Ensembl
Regulation of smooth muscle contraction Source: UniProtKB
Regulation of transcription, DNA-templated Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm. Predominantly localizes to the cytoplasm but can shuttle between the nucleus and cytoplasm; cytoplasmic localization is promoted by phosphorylation at Thr-299 and involves Rho/Rock signaling.
PTM
The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. Both isoform 1 and isoform 2 can undergo autophosphorylation.

Chen, H. M., & MacDonald, J. A. (2021). Molecular network analyses implicate death-associated protein kinase 3 (DAPK3) as a key factor in colitis-associated dysplasia progression. medRxiv.

Chen, H. M., Carlson, D. A., Haystead, T. A., & MacDonald, J. A. (2021). Death-associated protein kinase 3 (DAPK3) contributes to intestinal epithelial wound healing and the resolution of experimental colitis in mice. bioRxiv.

Chen, T. H. M. (2021). Death-associated Protein Kinase 3 (DAPK3), Identified as a Potential Key Factor for the Progression of Ulcerative Colitis (UC), Regulates Intestinal Epithelial Repair.

Li, G. M., Li, L., Li, M. Q., Chen, X., Su, Q., Deng, Z. J., ... & Bi, J. (2021). DAPK3 inhibits gastric cancer progression via activation of ULK1-dependent autophagy. Cell Death & Differentiation, 28(3), 952-967.

Li, K. X., Du, Q., Wang, H. P., & Sun, H. J. (2019). Death-associated protein kinase 3 deficiency alleviates vascular calcification via AMPK-mediated inhibition of endoplasmic reticulum stress. European Journal of Pharmacology, 852, 90-98.

Kake, S., Usui, T., Ohama, T., Yamawaki, H., & Sato, K. (2017). Death-associated protein kinase 3 controls the tumor progression of A549 cells through ERK MAPK/c-Myc signaling. Oncology Reports, 37(2), 1100-1106.

Mudry, J. M., Lassiter, D. G., Nylén, C., García-Calzón, S., Näslund, E., Krook, A., & Zierath, J. R. (2017). Insulin and glucose alter death-associated protein kinase 3 (DAPK3) DNA methylation in human skeletal muscle. Diabetes, 66(3), 651-662.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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