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The protein encoded by PLK2 is a member of the polo family of serine/threonine protein kinases that have a role in normal cell division. Additionally we are shipping Polo-Like Kinase 2 Antibodies (59) and Polo-Like Kinase 2 Kits (3) and many more products for this protein.
Showing 8 out of 10 products:
Human PLK2 Protein expressed in Wheat germ - ABIN1315438
Chen, Huang, Liu, Xu, Jiang: Design, synthesis, and evaluation of non-ATP-competitive small-molecule Polo-like kinase 1 (Plk1) inhibitors. in Archiv der Pharmazie 2015
Develop a DDS for continuous intracellular delivery of PLK2.
Structural analysis of the polo-box domain of human PLK2 has been presented.
our study demonstrates a novel mechanism of PLK2 in promoting tumor progression, whereby it directly binds to enriched TAp73 (show TP73 Proteins), catalyzes Ser48 phosphorylation of TAp73 (show TP73 Proteins), and inhibits TAp73 (show TP73 Proteins) transcriptional activity
Data suggest wild-type SNCA (alpha-synuclein) binding to synaptosome membrane is not affected by phosphorylation by PLK2; A30P SNCA, a Parkinson disease mutation, binding is greatly increased; endocytosis of SNCA fibrils follows similar pattern.
Decreased PLK2 protein expression due to promoter hypermethylation was negatively correlated with JAK2 (show JAK2 Proteins) overexpression, a common occurrence in hematological malignancies.
PLK2 SNPs were associated with Alzheimer disease and mild cognitive impairment. PLK2-rs15009 CC and GG genotypes and CC genotype at PLK2-rs702723 were protective for AD.
PLK2 indirectly activates ROCK2 (show ROCK2 Proteins) via phosphorylating nucleophosmin (show NPM1 Proteins) during centrosome amplification.
these findings reveal a conserved PLK2-RAP1 pathway that is crucial to regulate endothelial tip cell behavior in order to ensure proper vascular development and patterning in vertebrates.
Silencing of polo-like kinase 2 increases cell proliferation and decreases apoptosis in SGC (show SGCB Proteins)-7901 gastric cancer cells.
Unique PLK2-dependent protein phosphorylation sites identified by mass spectrometry.
These results support a significant role for a PLK kinase in phosphorylating alpha-synuclein at Ser129 in the brain, and suggest that PLK2 is responsible for this activity under physiological conditions.
In support of a tumor suppressor function for Plk2, loss of Plk2 increased the formation of lesions in multiparous glands. Collectively, these results demonstrate a novel role for Plk2 in regulating mammary gland development.
c-Fos and polo-like kinase 2 induction is impaired in the limbic system of fear-conditioned alpha-synuclein transgenic mice
PLK2 inhibition is a tractable CNS pharmacological target that does not cause genotoxicity at doses and exposures that engage the target in the sensory retina.
perturbation of Plk2 disrupts Ras and Rap (show LRPAP1 Proteins) signaling, prevents homeostatic shrinkage and loss of dendritic spines, and impairs proper memory formation.
CIB (show CIB1 Proteins) co-immunoprecipitated with Snk (show ATP1A4 Proteins) and inhibited the kinase activity of Snk (show ATP1A4 Proteins), suggesting that CIB (show CIB1 Proteins) is a negative regulator for Snk (show ATP1A4 Proteins) kinase activity.
there is a mitotic checkpoint (show BUB3 Proteins) wherein p53 (show TP53 Proteins)-dependent activation of Snk/Plk2 prevents mitotic catastrophe following spindle damage
PLK2 directly phosphorylates alpha-synuclein at Ser (show SIGLEC1 Proteins)-129 in an in vitro biochemical assay
Here we show that CHK-2 promotes pairing and synapsis by phosphorylating a family of zinc finger proteins that bind to specialized regions on each chromosome known as pairing centers, priming their recruitment of the Polo-like kinase PLK-2.
Polo kinases, via their polo box domains, bind to and regulate the activity of two key polarity proteins, MEX-5 and MEX (show ZSWIM2 Proteins)-6.
The protein encoded by this gene is a member of the polo family of serine/threonine protein kinases that have a role in normal cell division. This gene is most abundantly expressed in testis, spleen and fetal tissues, and its expression is inducible by serum, suggesting that it may also play an important role in cells undergoing rapid cell division. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
polo-like kinase 2
, serine/threonine-protein kinase PLK2
, Serine/threonine-protein kinase PLK2
, serine/threonine-protein kinase PLK2-like
, serine/threonine-protein kinase SNK
, serum-inducible kinase
, polo-like kinase 1