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TAO Kinase 2 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9UL54 |
|---|---|
| Other Accession | O94957 |
| Clone Names | 2040807 |
| Gene ID | 9344 |
|---|---|
| Other Names | Serine/threonine-protein kinase TAO2, Kinase from chicken homolog C, hKFC-C, Prostate-derived sterile 20-like kinase 1, PSK-1, PSK1, Prostate-derived STE20-like kinase 1, Thousand and one amino acid protein kinase 2, TAOK2, KIAA0881, MAP3K17, PSK, PSK1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7954a was selected from the C-term region of human TAOK2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | TAOK2 |
|---|---|
| Synonyms | KIAA0881, MAP3K17, PSK, PSK1 |
| Function | Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress- activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C- terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF- kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation. |
| Cellular Location | Cytoplasmic vesicle membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton Nucleus. Note=Catalytically active full-length phosphorylated isoform 1 localizes to microtubules in the cytoplasm predominantly on microtubule cables positioned around the nucleus. A C-terminally truncated form of isoform 1 is present in the nucleus; isoform 2 and kinase-defective, as well as full-length isoform 1 are excluded from the nucleus |
| Tissue Location | Ubiquitously expressed, with a higher level of expression in testis and brain. |
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Provided below are standard protocols that you may find useful for product applications.
Background
TAO kinase 2 (Serine/threonine-protein kinase TAO2) belongs to the MAP kinase family. It activates the JNK MAP kinase pathway through the specific activation of the MAP2Ks MEK3 and MEK6. TAO kinase 2 mediates signaling from carbachol, relaying signals from carbachol through heterotrimeric G proteins to the p38 MAP kinase and ternary complex factors. It alters actin cytoskeletal organization and interacts with microtubules affecting their organization and stability independently of TAO kinase activity.
References
Ota, T., et al., Nat. Genet. 36(1):40-45 (2004).Clark, H.F., et al., Genome Res. 13(10):2265-2270 (2003).Chen, Z., et al., J. Biol. Chem. 278(25):22278-22283 (2003).Mitsopoulos, C., et al., J. Biol. Chem. 278(20):18085-18091 (2003).Moore, T.M., et al., J. Biol. Chem. 275(6):4311-4322 (2000).
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