Recombinant Human PLK1 Protein

Name: Recombinant Human PLK1 Protein
Brand: Beta LifeScience
SKU: BL-0957SG
Availability: InStock

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Product Overview

Tag	His
Host Species	Human
Accession	NM_005030
Synonym	STPK13
Background	PLK1 is a member of the Polo-Like Kinase family that localize to centrosomes or spindle pole bodies and undergo dramatic subcellular relocation during the cell cycle. Deregulated activities of PLKs often result in abnormalities in centrosome duplication, maturation, and/or microtubule dynamics (1). PLKs also regulate the function of the Golgi complex. Deregulated expression of human PLK1 is strongly correlated with the development of many types of malignancies, and ectopic expression of PLK1 dominant negative protein leads to rapid cell death (2).
Description	Recombinant full-length human PLK1 was produced by baculovirus in Sf9 insect cells using a N-terminual His tag. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	~70 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human PLK1 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning. Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage. Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression. Regulates mitotic progression by phosphorylating RIOK2.
Subcellular Location	Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody.
Protein Families	Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
Database References	HGNC: 9077 OMIM: 602098 KEGG: hsa:5347 STRING: 9606.ENSP00000300093 UniGene: Hs.592049
Associated Diseases	Defects in PLK1 are associated with some cancers, such as gastric, thyroid or B-cell lymphomas. Expression is cancer increased in tumor tissues with a poor prognosis, suggesting a role in malignant transformations and carcinogenesis.
Tissue Specificity	Placenta and colon.

Gene Functions References

Plk1 overexpression has tumor-suppressive properties by perturbing mitotic progression and cytokinesis. PMID: 30069007
These findings indicate that PLK1 might be a potential therapeutic target for the treatment of sepsis-induced intestinal barrier dysfunction. PMID: 29348559
a transcription-independent mechanism for Stat3-mediated centrosome clustering that involves Stathmin, a Stat3 interactor involved in microtubule depolymerization, and the mitotic kinase PLK1, is reported. PMID: 28474672
expression in oral squamous cell carcinoma and oral submucous fibrosis PMID: 29652009
Analyses with phospho-defective and phospho-mimetic mutants of FoxM1b identified a critical role of the Plk1 phosphorylation sites in regulating the binding of FoxM1b to Rb and DNMT3b. PMID: 28387346
A significant over expression of forkhead box protein M1 (FOXM1), polo-like kinase 1 (PLK1) and centrosomal protein 55 (CEP55) was observed in tumor samples compared to adjacent and normal bladder tissues, suggesting they may be potential candidate's biomarkers for early diagnosis and targets for cancer therapy. PMID: 30277841
The results of the study suggest that miR23a inhibits pancreatic cancer (PC) cell progression by directly targeting PLK1associated signaling and promoting miR23a expression may be a potential method for treating patients with PC. PMID: 29749476
TPX2 promotes the proliferation and migration of human OC cells by regulating PLK1 expression. PMID: 29865033
Findings indicate a critical role for Polo-like kinase 1 (Plk1) in regulating biosynthesis in cancer cells. PMID: 29138396
Observations demonstrated that Plk1 directly interacts with RNF2 and degrades RNF2 via the ubiquitindependent degradation pathway. PMID: 29565459
PLK1 was upregulated in the SGC-7901/DDP (cisplatin-resistant) gastric cancer cells compared with the SGC-7901 cells. PMID: 29393385
let-7b targets PLK1 to inhibit hepatocellular carcinoma cell growth and induce their apoptosis by attenuating the PLK1-mediated Survivin phosphorylation PMID: 29913237
an elevated PLK1 level significantly predicted unfavorable overall survival (hazard ratio = 1.78, 95% CI: 1.10-2.88, P = 0.019) and was correlated with female gender (OR = 0.73, 95% CI: 0.56-0.95, P = 0.017), tumor thrombus (OR = 3.97, 95% CI: 1.46-10.78, P < 0.001), metastasis (OR = 3.46, 95% CI: 1.33-9.01, P = 0.011), pathologic stage (OR = 1.56, 95% CI: 1.17-2.07, P = 0.002). PMID: 29843122
that SUMOylation is an important regulatory mechanism governing PLK1's mitotic function PMID: 29166606
The authors show that human Cyclin-Dependent-Kinases (CDKs) target the RAD9 subunit of the 9-1-1 checkpoint clamp on Thr292, to modulate DNA damage checkpoint activation. Thr292 phosphorylation on RAD9 creates a binding site for Polo-Like-Kinase1 (PLK1), which phosphorylates RAD9 on Thr313. PMID: 29254517
hnRNPK regulates PLK1 expression by competing with the PLK1-targeting miRNAs, miR-149-3p and miR-193b-5p. PMID: 28708135
The expression of APC-DeltaC in colon cells reduces the accumulation of mitotic cells upon PLK1 inhibition, accelerates mitotic exit and increases the survival of cells with enhanced chromosomal abnormalities. PMID: 29549256
Polo-like kinase inhibition can sensitize cholangiocarcinoma cells to cisplatin-induced apoptosis with proteasomal Bcl-2 degradation as an additional pro-apoptotic effect. PMID: 28652654
Results showed that Polo-like kinase 1 (Plk1) plays an important role in the conversion of cancer stem cells (CSCs) between active and quiescent states. PMID: 28430578
Authors demonstrated that WDR62 is a PLK1 substrate that is phosphorylated at Ser 897, and that this phosphorylation at the spindle poles promotes astral microtubule assembly to stabilize spindle orientation. PMID: 28973348
findings thus elucidate a critical role for Plk1 in CyclinB1-Cdk1 activation and mitotic entry and outline how CyclinA2-Cdk, an S-promoting factor, poises cells for commitment to mitosis. PMID: 28591578
Data show that a microRNA-mimic to increase miR-34a together with siRNA to silence PLK1 oncogene prolonged survival. PMID: 29295989
PLK1 inhibitors may be effective for patients with high-risk or relapsed neuroblastomas with upregulated PLK1. PMID: 28036269
The authors found that SYP-4 is phosphorylated dependent on Polo-like kinases PLK-1/2. They propose a model in which Polo-like kinases recognize crossover designation and phosphorylate SYP-4 thereby stabilizing the synaptonemal complex and making chromosomes less permissive for further double-strand break formation. PMID: 28346135
Data suggest that FBXW7, MCL1 and PLK1 may be relevant predictive markers of tumor progression and response to paclitaxel treatment. PMID: 27409838
we have identified lnc-RI as a new regulator of mitosis which acts by releasing PLK1 mRNA activity via competition for binding to miRNA-210-3p. PMID: 27160062
A FAK-Src signaling pathway downstream of integrin-mediated cell adhesion was found to decelerate both PLK1 degradation and CEP55 accumulation at the midbody. These data identify the regulation of PLK1 and CEP55 as steps where integrins exert control over the cytokinetic abscission. PMID: 27127172
Data indicate that the mitotic kinase Polo-like kinase 1 (PLK1) was an important effector of S1P-S1P5 signaling, and a new function of the SphK1-S1P pathway specifically in the control of mitosis in HeLa cells. PMID: 28351953
proviral action associated with biogenesis of the nucleocapsid PMID: 28445592
identified Polo-like kinase 1 (PLK1), a major signaling hub in the spindle subnetwork, as phosphorylated at the conserved Tyr(217) in the kinase domain. Substitution of Tyr(217) with a phosphomimetic residue eliminated PLK1 activity in vitro and in cells. PMID: 27965426
PLK1 inhibition mitigates autophagy in cancer cells both under nutrient starvation and sufficiency, and a role of PLK1 in autophagy is also observed in the invertebrate model organism Caenorhabditis elegans. PMID: 28102733
a novel p53-independent regulation of PLK1 during CRC differentiation and apoptosis. PMID: 28341486
Results show that PLK1 is overexpressed in diffuse intrinsic pontine gliomas. PMID: 27538997
Mutant IDH1 promotes checkpoint adaptation which can be exploited therapeutically with the combination of TMZ and a PLK1 inhibitor, indicating PLK1 inhibitors may be clinically valuable in the treatment of IDH1 mutant gliomas PMID: 28178660
Genistein induced mitotic arrest by inhibiting Plk1 activity and, consequently, led to mitotic catastrophe and apoptosis. Tumor cells with TP53 mutations were more sensitive to cell death by treatment of genistein. PMID: 27861885
we show that Plk1 phosphorylates Mre11 at S649 during G2 DNA damage recovery and Mre11 phosphorylation at S649/S689 drives premature checkpoint termination and reduced DNA repair PMID: 28512243
We propose that the DDR targets recruitment of Aurora A to the Plk1/Bora complex to prevent activation of Plk1 during DNA damage in G2. PMID: 27721411
Studies provide evidence that PLK1 plays a role during cell cycle progression and human pediatric cancer. [review] PMID: 26302797
Small molecule inhibition of polo-like kinase 1 by volasertib (BI 6727) causes significant melanoma growth delay and regression in vivo. PMID: 27793694
Mutations of the LIM protein AJUBA mediate sensitivity of head and neck squamous cell carcinomas to treatment with PLK1 inhibitors. PMID: 28126323
PLK1 may be an important regulator of metabolism maintenance in melanoma cells. PMID: 28235541
The authors show that a global spread of ATM activity on chromatin and phosphorylation of ATM targets including KAP1 control Plk1 re-activation. These phosphorylations are rapidly counteracted by the chromatin-bound phosphatase Wip1, allowing cell cycle restart despite persistent ATM activity present at DNA lesions. PMID: 28607002
These data implicate the insulin-FoxM1/PLK1/CENP-A pathway-regulated mitotic cell-cycle progression as an essential component in the beta cell adaptation to delay and/or prevent progression to diabetes. PMID: 28286049
Inhibition of PLK1 activity or overexpression of a non-phosphorylatable PLK1 mutant reduces the polyploid cell population. PMID: 27398835
the mechanism of Plk1 activation and the potential role of Bora phosphorylation by Cdk1, is reported. PMID: 27831827
centrosome maturation occurs during interphase in an MLK-dependent manner, independent of the classic mitotic kinase, Plk1. PMID: 27219065
High PLK1 expression is associated with hepatocellular carcinoma. PMID: 28267710
centrosome protein Dzip1 mediates the assembly of the BBSome-Dzip1-PCM1 complex in the centriolar satellites (CS) at the G0 phase for ciliary translocation of the BBSome. Phosphorylation of Dzip1 at Ser-210 by Plk1 (polo-like kinase 1) during the G2 phase promotes disassembly of this complex, resulting in removal of Dzip1 and the BBSome from the CS. PMID: 27979967
miR-509-3-5p is a strong suppressor of cancer via targeting PLK1. PMID: 27498003
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin phosphorylation at Ser-56. PMID: 27662907

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