|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for PLK1(NM_005030.5) Search again
Product ID:
HQP104670
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
PLK, STPK13
Gene Description:
polo like kinase 1
Target Gene Accession:
NM_005030.5(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Gene References into function
- We have observed that overexpression of the C-terminal domain of Plk is more effective than wild-type or kinase-defective Plk in causing mitotic delay or arrest.
- results suggest that Plk1 phosphorylates Cdc25C on Ser198 and regulates nuclear translocation of Cdc25C during prophase
- These results suggest that Polo-like kinase regulates the dissociation of cohesin from chromosomes early in mitosis. (cohesin)
- both PB1 and PB2 regions are required for targeting the catalytic activity of Plk1 to centrosomes, midbody, and kinetochores
- role of depletion in activating Cdc2/cyclin B and inhibition of centrosome amplification
- Downregulation of cellular PLK1 levels in cancer cells altered cell cycle progression moderately with an elevated percentage (20-30%) of cells in G(2)/M. Furthermore, cells with reduced PLK1 protein gained a rounded phenotype with multiple centrosomes.
- Plk1 kinase is involved in regulation of cyclin B1 phosphorylation and inhibited by ATR
- Ser-137 may have an unexpected and novel role in the function of Plk
- accumulates in both the nucleus and the cytoplasm in addition to its localization to the centrosome during S and G(2) phases
- promoter elements responsible for transcriptional inhibition of polo-like kinase 1 and topoisomerase IIalpha genes by p21(WAF1/CIP1/SDI1)
- A site corresponding to Ser326 in Plx1 was shown to be phosphorylated in the human polo-like kinase Plk1 (Ser335)
- role in regulating subcellular localization of cyclin B1
- interaction with Chk2 and localization to centrosomes and midbody
- Suppression of the activity of PLK1 via inhibition of tyrosine kinase activity by beta-HIVS might play a critical role in the induction of apoptosis.
- identified the polo-box domain (PBD) of the mitotic kinase polo-like kinase 1 as a specific phosphoserine or phosphothreonine binding domain and determined its optimal binding motif
- PLK1 overexpression was significantly associated with p53 accumulation in colorectal cancers. Our results suggest overexpression of PLK1 might be of pathogenic, prognostic and proliferative importance.
- Depletion of this enzyme induces apoptosis in cancer cells
- a consensus motif for Plk (Polo-like kinase) phosphorylation is identified, and Myt1 is a Plk1 substrate
- Plk1 phosphorylates BRCA2 in M phase
- PLK1 regulates Nlp, a centrosome protein involved in microtubule nucleation.
- PLK1 phosphorylation of NudC plays an essential role in cytokinesis.
- Data suggest that phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 (Plk1) is necessary for the restriction of Plk1 to the spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis.
- Data show that the Polo-box domains of human, Xenopus, and yeast polo-like kinases all recognize similar phosphoserine/threonine-containing motifs
- crystal structure of Plk1 polo box domain provides an explanation for phospho-peptide recognition
- Cell cycle arrest at G2/M after ionizing radiation (IR) of breast carcinoma cells may involve repression of the gene for Plk1.
- A putative destruction box in Plk1 is required for degradation of Plk1 in anaphase.
- PLK1 does not act as a cell cycle regulator but plays a constitutive role in papillary carcinoma especially in the early phase, and may contribute to the malignant transformation of this carcinoma
- PLK1 regulates the cell cycle progression of thyroid lymphoma cells in the G2-M-phase.
- p53 is a critical target of Plk1, and its function is abrogated through the physical interaction with Plk1.
- Data demonstrate that Plk1 (Polo-like kinase 1) is a target of the retinoblastoma tumor suppressor (RB) pathway.
- Mitotic phosphorylation of Nir2 is required for docking of the phospho-Ser/Thr binding module, the Polo box domain of Plk1, and overexpression of a Nir2 mutant, which fails to interact with Plk1, affects the completion of cytokinesis.
- Antisense-treated pancreatic cancer cells showed cell cycle arrest in G(2)-M as well as a drastic reduction in proliferation rates
- High rate of PLK-1 positivity seen in prostate cancer; PLK1 may be involved in prostate cancer tumorigenesis and progression
- the role of Plk1 in mitosis regulation through the identification of Ser-4 in B23 nucleophosmin as a major physiological substrate of Plk1
- Plk1 and CHO1/MKLP-1 interact to have a role in cytokinesis
- Plk1 has a role in bipolar spindle formation but is not necessary for APC/C-Cdc20 activation and initiation of cytokinesis
- Treatment of mitotic cells with DNA damaging agents inhibits Plk1 activity primarily through dephosphorylation of Plk1.
- The cell cycle machinery is reset in response to DNA damage and that cells become critically dependent on Plk1-mediated degradation of Wee1 for their recovery.
- Plk-1 is required for proper spindle assembly and function.
- Plk1 activates the anaphase promoting complex by directing the SCF-dependent destruction of Emi1 in prophase
- in vivo phosphorylation of Plk1 at serine 137 (S137) and threonine 210 (T210) occurs in mitosis; DNA damage prevents phosphorylation of Plk1 at both S137 and T210 in asynchronous cells but not in mitotic cells
- Cep170 interacts with Polo-like kinase 1 in mature centrioles
- interaction between endogenous Plk1 and Mcm7 was detected in a soluble chromatin fraction. These findings suggest a new function for Plk1 in coordination of DNA replication and mitotic events.
- phosphorylation of HSF1 by PLK1 is an essential step for HSF1 nuclear translocation by heat stress
- study suggested that polo-like kinase 1 (Plk1) plays a critical role in the process of prostate cancer development
- The polo-like kinase 1 activity and expression in complex proteomes is rapid detection by AX7503.
- Plk1-dependent signalling mechanism potentially linking Golgi structure and cell cycle control
- Plk1 function is altered at different stages of mitosis through phosphorylation of Ser-137 and Thr-210.
- PLK1 was found overexpressed in pancreatic neoplasia as early as in pancreatic intraepithelial neoplasia III lesions, whereas benign acinar pancreatic parenchyma and ductal epithelia showed only focal PLK1 positivity.
- Plk1 Polo box domain mediates a cell cycle and DNA damage regulated interaction with Chk2
- Data show that Plk1 associates with chaperonin-containing TCP1 complex (CCT) both in vitro and in vivo.
- Study suggests that PLK1 expression significantly reflects aggressive characteristics of medullary thyroid carcinoma.
- DNA damage-induced inhibition of Plk1 leads to inhibition of Nek2 activity and thus prevents centrosome separation
- Results highlight the centrosome as a site to organize phosphorylation of Cep55 by Erk2/Cdk1 and Plk1, enabling it to relocate to the midbody to function in mitotic exit and cytokinesis.
- The expression patterns and prognostic implications of the mitotic regulator Polo-like kinase 1 in colon cancer are reported.
- ECT2 is regulated by Plk1
- Plk1 helps to coordinate changes in microtubule organization with cell cycle progression, by controlling the dynein-dynactin-dependent transport of centrosomal proteins.
- Cdk1 regulated mitotic vimentin phosphorylation via not only a direct enzyme reaction but also Plk1 recruitment to vimentin.
- whereas chromosome congression requires localized Plk1 activity, other investigated Plk1 functions are less dependent on correct polo-box domain-mediated targeting
- The complex formation of Plk1 and Aurora-B on INCENP may play crucial roles in the regulation of chromosomal dynamics.
- the Polo box domain of Plk3 is more potent in inhibiting cell proliferation and inducing apoptosis than that of Plk1
- The polo box domain in complex with a phosphorylated peptide is examined crystallographically.
- Overexpression of PLK1 is associated with gastric cancer
- Phosphorylation of cdc25c can be used to test whether a pharmacologic inhibitor of Plk1 would exert the same cellular effects as interference with Plk1 on an mRNA level.
- Cdc25C may first be actived by Plk1, and then its phosphatase activity makes p53 dephosphorylated at Ser15
- Phosphorylation of Bub1 at T609 by Cdk1 creates a docking site for the PBD of Plk1 and facilitates the kinetochore recruitment of Plk1.
- Tumors with PLK1 overexpression were associated more frequently with CIN, DNA aneuploidy and centrosome amplification. Overexpression of PLK1 was significantly related to higher pathological grade, multiple tumors and positive urine cytology.
- NudC functions as both a substrate and a spatial regulator of Plk1 at the kinetochore to promote chromosome congression.
- Overexpression of Polo-like kinase 1 is associated with human gastric carcinomas
- Checkpoint kinase 1 (Chk1) is required for mitotic progression through negative regulation of polo-like kinase 1 (Plk1)
- Either chk1 or plk1-specific antisense oligodeoxynucleotides enhanced DNA damaging agent-induced apoptosis.
- Plk1 regulates the spindle organization partially through its phosphorylation on Ran
- The degradation of Claspin upon mitotic entry depends on Plk1.
- We propose that hCenexin1 is a critical centrosomal component whose C-terminal extension is required for proper recruitment of Plk1 and other components crucial for normal mitosis.
- Intranuclear OPN participates in the process of cell duplication and associates with Plk1
- Plk1 self-regulates the Plk1-PBIP1 interaction to timely localize to the kinetochores and promote proper chromosome segregation.
- Plk1 has a role in mitotic arrest, which is released by Chk1
- a nitric oxide-p38 MAPK-p21/Waf1 signal transduction pathway represses PLK1 through a canonical CDE/CHR promoter element
- a novel pathway, which is connected between ataxia telangiectasia-mutated kinase (ATM) and protein phosphatase-Plk1 in DNA damage response in mitosis
- These data identify PICH as a novel essential component of checkpoint signaling.
- correlation between COX-2 and PLK-1 in a malignant prostate tumor
- TTDN1 is phosphorylated in mitosis, and this is required for its interaction with polo-like kinase 1.
- Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1.
- siRNA-induced suppression of Plk1 expression effectively reduced the viable cell mass and increased apoptosis in several cancer cell lines
- Results suggest that an onocogenic role of overexpressed cyclin B1 is mainly mediated in nuclei of breast carcinoma cells, and the nuclear translocation is regulated by polo-like kinase 1 and 14-3-3sigma.
- Polo-like kinase 1 has a role in positioning RhoA and triggering cytokinesis in human cells
- Plk1 facilitates chromosome alignment during prometaphase through BubR1.
- These findings suggest that PLK-1 plays a critical role in the proliferation of RA synoviocytes leading to bone destruction, and siRNA against PLK-1 is potentially useful for the treatment of RA.
- Plk1 and RhoA function to enhance Rock2 kinase activity in vitro and within cells, and implicate Plk1 as a regulator of multiple pathways that synergistically converge to regulate actomyosin ring contraction during cleavage furrow ingression.
- Crystallized structures of Plk1 reveal the typical kinase fold with the unphosphorylated activation loop in an extended conformation, stabilized by a crystal contact.
- Late mitotic Plk1 activity promotes recruitment of Ect2 to the central spindle, triggering the initiation of cytokinesis and contributing to cleavage plane specification in human cells.
- New work has now identified PRC1 as a Plk1-delivery factor that is tightly controlled by opposing cyclin B-Cdk1- and Plk1-dependent phosphorylations.
- Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1.
- PLK1-HsCdc14A interaction provides a temporal regulation of HsCdc14A in chromosome segregation during mitosis.
- Co-immunoprecipitation reveals that RhoA and polo-like kinase 1 physically interact and that their interaction appears to be enhanced during mitosis.
- Plk1 activity is essential for cleavage furrow formation and ingression, leading to successful cytokinesis.
- Compared with survivin, PLK1 seems to be a better independent prognostic factor for diffuse large B-cell lymphoma.
- Over expression of Polo-like kinase 1 is associated with preinvasive in situ carcinomas of the breast
- topoisomerase IIalpha is a novel physiological substrate for Plk3, and Plk1 and Plk3 play different roles in cell-cycle regulation.
- Plk1-dependent phosphorylation regulates functions of DNA topoisomerase IIalpha in cell cycle progression
- Plk1-mediated dysfunction of p73 is one of the novel molecular mechanisms to inhibit the p53-independent apoptosis
- Plk1 phosphorylation of Hbo1 may be required for prereplicative complex (pre-RC) formation and DNA replication licensing
- Plk1 inhibition could significantly inhibit cell proliferation and induce cell cycle arrest and apoptosis
- cancer cell lines have a much greater requirement for Plk1 than normal nontransformed diploid cells
- Phosphorylation and the presence of the PBD-binding phosphopeptide result in an increase in catalytic efficiency of 1515x with a 2.3-fold decrease in K(M) and a 705-fold increase in k(cat) over the unmodified Plk1.
- Centriole splitting induced by Sgo1 depletion or expression of a dominant negative mutant is suppressed by ectopic expression of sSgo1 or by Plk1 knockdown.
- Proteolysis of Bora requires the Plk1 kinase activity and is mediated by SCF-beta-TrCP; Plk1 phosphorylates a conserved DSGxxT degron in Bora and promotes its interaction with beta-TrCP.
- the first crystal structure of the kinase domain of wild-type apo Plk-1, in complex with designed ankyrin-repeat proteins, is presented
- TAp73-mediated activation of the p21(cip/waf), 14-3-3sigma and Bax gene promoters is abrogated by expressed PLK1 for which post-translational modification of TAp73 Thr-27 appears to be a key step in MCF7 cells.
- activity is regulated by p21-activated kinase and leads to mitotic progression
- These results identify a previously unrecognized role for MYPT1 in regulating mitosis by antagonizing PLK1.
- Plk1 controls Aurora A localization and function by regulating cellular levels of hBora.
- PLK1 overexpression is an adverse predictive factor in NHL
- Plk1 is phosphorylated in the starting M-phase, and this phosphorylation induces polo-box targeting through a possible conformational change.
- study reports that the synergistic action of Bora & the kinase Aurora A controls G2-M transition; Bora accumulates in G2 phase & promotes Aur-A-mediated activation of Polo-like kinase 1, leading to activation of cyclin-dependent kinase 1 & mitotic entry
- data demonstrate that the initial activation of PLK1 is a primary function of aurora A
- in U937 AML cells, PLK1 participates in checkpoint recovery, and that inhibition of PLK by the GW843682X compound results in mitotic accumulation and apoptosis
- Plk1 interacts with and phosphorylates TRF1 and Plk1-mediated phosphorylation is involved in both TRF1 overexpression-induced apoptosis and its telomeric DNA binding ability
- In response to genotoxic stress in G2, the phosphatase Cdc14B translocates from the nucleolus to the nucleoplasm and induces the activation of the ubiquitin ligase APC/C(Cdh1), with the consequent degradation of Plk1, a prominent mitotic kinase.
- Plk1 can regulate MyoGEF activity and localization, contributing to the regulation of cytokinesis
- Only Plk1-S326E, but not the Plk1-S326A, efficiently rescued the p38 or MK2-depletion-induced mitotic defects, further solidifying the requirement of S326 phosphorylation during mitotic progression
- These observations suggest that Plk1 is a regulator of Bcl-x(L) phosphorylation and controls the anti-apoptotic activity of Bcl-x(L) during pironetin-induced apoptosis.
- mechanistic roles contributed by protein phosphorylation and Plk1 to the spindle assembly checkpoint activity of Mad1
- Regulation of I(kappa)B kinase complex by phosphorylation of (gamma)-binding domain of I(kappa)B kinase (beta) by Polo-like kinase 1.
- Metastatic HCC cells showed a defective S-M checkpoint following cisplatin treatment and potential aberrant checkpoint adaptation, which might result from deregulation of Plk1-Cdc25A pathway.
- PLK1 might be a useful prognostic marker and a potential therapeutic target for esophageal squamous cell carcinoma
- demonstrate the predominant role of polo box domain-dependent binding on smooth chromosome congression at metaphase
- Through a yeast two-hybrid screening, human polo-like kinase 1 was found to interact with human papillomavirus type 5 E2.
- Plk1-dependent regulation of FoxM1 activity provides a positive-feedback loop ensuring tight regulation of transcriptional networks essential for orderly mitotic progression.