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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 Proteins (12) and many more products for this protein.
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Findings indicate the interaction network of viral oncogene (show RAB1A ELISA Kits) HPV16 E7, miR (show MLXIP ELISA Kits)-27b and PLK2, and support the potential strategies using antisense nucleic acid of miR (show MLXIP ELISA Kits)-27b for therapy of cervical cancer.
CHOP (show DDIT3 ELISA Kits) negatively regulates Polo-like kinase 2 expression via recruiting C/EBPalpha (show CEBPA ELISA Kits) to the upstream-promoter in human osteosarcoma cell line during ER stress
Plk2 represents an independent prognostic marker and regulates tumor growth and apoptosis by targeting Fbxw7 (show FBXW7 ELISA Kits)/Cyclin E (show CCNE1 ELISA Kits) pathway in colorectal carcinoma.
PLK2 kinase has a role in mediating alpha-synuclein selective autophagic degradation
PLK2, functional kinase and polo (show PLK1 ELISA Kits)-box domains were required for interaction with PFV Gag. Fluorescently-tagged PFV Gag, through its chromatin tethering function, selectively relocalized ectopically expressed eGFP-tagged PLK (show PLK1 ELISA Kits) proteins to mitotic chromosomes i
Develop a DDS for continuous intracellular delivery of PLK2.
Structural analysis of the polo (show PLK1 ELISA Kits)-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 ELISA Kits), catalyzes Ser48 phosphorylation of TAp73 (show TP73 ELISA Kits), and inhibits TAp73 (show TP73 ELISA Kits) 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 ELISA Kits) overexpression, a common occurrence in hematological malignancies.
miR-146a regulates lineage negative bone marrow cell senescence and apoptosis by suppressing Plk2 expression that, in turn, activates p16Ink4a/p19Arf and p53 signaling.
These results support a significant role for a PLK (show PLK1 ELISA Kits) 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 ELISA Kits) signaling, prevents homeostatic shrinkage and loss of dendritic spines, and impairs proper memory formation.
CIB co-immunoprecipitated with Snk and inhibited the kinase activity of Snk, suggesting that CIB is a negative regulator for Snk kinase activity.
there is a mitotic checkpoint wherein p53 (show TP53 ELISA Kits)-dependent activation of Snk/Plk2 prevents mitotic catastrophe following spindle damage
PLK2 directly phosphorylates alpha-synuclein at Ser (show SIGLEC1 ELISA Kits)-129 in an in vitro biochemical assay
The authors found that SYP (show SYP ELISA Kits)-4 is phosphorylated dependent on Polo (show PLK1 ELISA Kits)-like kinases PLK-1 (show PLK1 ELISA Kits)/2. They propose a model in which Polo (show PLK1 ELISA Kits)-like kinases recognize crossover designation and phosphorylate SYP (show SYP ELISA Kits)-4 thereby stabilizing the synaptonemal complex and making chromosomes less permissive for further double-strand break formation.
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 (show PLK1 ELISA Kits)-2.
Polo kinases, via their polo box domains, bind to and regulate the activity of two key polarity proteins, MEX-5 and MEX-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.
, serine/threonine-protein kinase PLK2
, serine/threonine-protein kinase SNK
, serum-inducible kinase
, polo-like kinase 1
, polo-like kinase 2 (Drosophila)
, polo-like kinase 2
, Serine/threonine-protein kinase PLK2
, serine/threonine-protein kinase PLK2-like