|Other Names||Serine/threonine-protein kinase VRK1, Vaccinia-related kinase 1, VRK1|
|Target/Specificity||The synthetic peptide is selected from the sequence of human VRK1 within aa 300-400.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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.|
|Function||Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr- 18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity.|
|Cellular Location||Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis|
|Tissue Location||Widely expressed. Highly expressed in fetal liver, testis and thymus.|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the vaccinia-related kinase (VRK) family of serine/threonine protein kinases. This gene is widely expressed in human tissues and has increased expression in actively dividing cells, such as those in testis, thymus, fetal liver, and carcinomas. Its protein localizes to the nucleus and has been shown to promote the stability and nuclear accumulation of a transcriptionally active p53 molecule and, in vitro, to phosphorylate Thr18 of p53 and reduce p53 ubiquitination. This gene, therefore, may regulate cell proliferation. This protein also phosphorylates histone, casein, and the transcription factors ATF2 (activating transcription factor 2) and c-JUN.
Blume-Jensen P, et al. Nature 2001. 411: 355.Cantrell D, J. Cell Sci. 2001. 114: 1439.Jhiang S Oncogene 2000. 19: 5590.Manning G, et al. Science 2002. 298: 1912.Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.Robertson, S. et al. Trends Genet. 2000. 16: 368.Robinson D, et al. Oncogene 2000. 19: 5548.Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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