PLK4 Antibody

Code CSB-PA018196XA01phHU
Size US$166
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Product Details

Uniprot No.
Target Names
PLK4
Alternative Names
Serine/threonine-protein kinase PLK4Curated (EC:2.7.11.213 Publications), Polo-like kinase 4, PLK-4, Serine/threonine-protein kinase 18, Serine/threonine-protein kinase Sak, PLK4Imported, SAK, STK18
Species Reactivity
Homo sapiens (Human)
Immunogen
Recombinant Homo sapiens PLK4 protein (301-313aa )
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Protein G
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification. Phosphorylates CEP131 at 'Ser-78' and PCM1 at 'Ser-372' which is essential for proper organization and integrity of centriolar satellites.
Gene References into Functions
  1. Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly. PMID: 29712910
  2. KAT2A/2B acetylation of PLK4 prevents centrosome amplification PMID: 27796307
  3. PLK4 played important roles in regulating cell cycle- and DNA replication-related pathways. E2F could upregulate the expression levels of PLK4 by deregulating the methylations of their promoters to promote the relapse of Acute Lymphoblastic Leukemia. PMID: 29768346
  4. PLK4 specifically phosphorylates CP110 at the S98 position and is an essential step for centriole assembly. PMID: 28562169
  5. These data show that complementary mechanisms, such as mother-daughter centriole proximity and CDK1-CyclinB interaction with centriolar components, ensure that centriole biogenesis occurs once and only once per cell cycle, raising parallels to the cell-cycle regulation of DNA replication and centromere formation. PMID: 27112295
  6. Homozygous splicing acceptor site transition (c.31-3 A>G) in PLK4 was identified in a family with Seckel syndrome. PLK4 is essential for centriole biogenesis and DNA damage response. PMID: 28832566
  7. the interaction between Cep78 and the N-terminal catalytic domain of Plk4 is a new and important element in the centrosome overduplication process. PMID: 27246242
  8. Our results validate Plk4 as a therapeutic target in cancer patients PMID: 27872092
  9. Heterozygous missense mutation in PLK4 identified in a patient with microcephaly and chorioretinopathy. Aberrant spindle formation was observed in a LCL derived from this patient. Mutant PLK4 proteins demonstrated altered mobility pattern on a western blot suggesting alterations in post-translation modification. PMID: 27650967
  10. Studies indicate that depletion of any one of the protein kinase polo-like kinase 4 (PLK4) and the two proteins STIL and SAS-6 blocks centriole duplication, and, conversely, overexpression causes centriole amplification. PMID: 27911707
  11. Common PLK4 variant rs2305957 is associated with blastocyst formation and early recurrent miscarriage in Chinese women. PMID: 28238495
  12. Mutations in human PLK4, the protein of which plays critical role in centriole duplication and normal nuclear formation, could be associated with abnormal spermatogenesis leading to Sertoli cell-only syndrome. Aberrant forms of PLK4 might also cause other types of oligozoospermia or sperm fl agellar abnormalities. PMID: 26452337
  13. Plk4 directly binds PCM1 and phosphorylates S372. Plk4 depletion leads to the dispersal of centriolar satellites. PMID: 26755742
  14. Decreased PLK4 protein expression due to promoter hypermethylation was negatively correlated with JAK2 overexpression, a common occurrence in hematological malignancies. PMID: 25347426
  15. KLF14 transcription is significantly downregulated, whereas Plk4 transcription is upregulated in multiple types of cancers, and there exists an inverse correlation between KLF14 and Plk4 protein expression in human breast and colon cancers. PMID: 26439168
  16. The authors suggest that the STIL-coiled-coil region/PLK4 interaction mediates PLK4 activation as well as stabilization of centriolar PLK4 and plays a key role in centriole duplication. PMID: 26188084
  17. We demonstrate that centrioles promote PLK4 activation through its recruitment and local accumulation. Though centriole removal reduces the proportion of active PLK4, this is rescued by concentrating PLK4 to the peroxisome lumen PMID: 26481051
  18. these results identify the interaction between Mib1 and Plk4 as a new and important element in the control of centriole homeostasis. PMID: 25795303
  19. PLK4 functions downstream of ROCK2 to drive centrosome amplification in arrested cells. PMID: 25590559
  20. PLK4 overexpression induces centrosome amplification and chromosome instability and causes the suppression of primary cilia formation. PMID: 24981932
  21. Negative feedback by centriolar STIL regulates bimodal centriolar distribution of Plk4 and seemingly restricts occurrence of procentriole formation to one site on each parental centriole. PMID: 25342035
  22. An unexpected activity of Plk4 that promotes cell migration and may underlie an association between increased Plk4 expression, cancer progression and death from metastasis in solid tumor patients. PMID: 25174401
  23. Plk4 activity promotes the recruitment of STIL to the centriole and primes the direct binding of STIL to the C terminus of SAS6. PMID: 26101219
  24. Mutation in PLK4, encoding a master regulator of centriole formation, defines a novel locus for primordial dwarfism. PMID: 25320347
  25. Data suggest polo-like kinase 4 (PLK4) inhibitors as a clinical candidate for cancer therapy. PMID: 25723005
  26. Studies indicate that overexpression of polo-like kinase 4 (PLK4) is found in several cancer and suggest the PLK4 inhibitors as anticancer therapeutics. PMID: 24867403
  27. identified association between aneuploidy of putative mitotic origin and linked genetic variants on chromosome 4 of maternal genomes; associated region contains candidate gene,PLK4, that plays a role in centriole duplication and can alter mitotic fidelity upon minor dysregulation PMID: 25859044
  28. different levels of impaired PLK4 activity result in growth and cilia phenotypes, providing a mechanism by which microcephaly disorders can occur with or without ciliopathic features PMID: 25344692
  29. Results demonstrated that Plk4 is under the direct control of the E2F activators in breast cancer cells. PMID: 24797070
  30. p53-Dependent and cell specific epigenetic regulation of the polo-like kinases under oxidative stress. PMID: 24498222
  31. Breast cancer cell viability is dependent on PLK4 expression. PMID: 25043604
  32. Plk4 is intricately regulated in time and space through ordered interactions with two distinct scaffolds, Cep192 and Cep152, and a failure in this process may lead to human cancer. PMID: 24997597
  33. it appears that Nek2 and Plk4 might synergize to promote breast tumorigenesis and may also be involved in tamoxifen and trastuzumab resistance PMID: 24389189
  34. PLK4 is a new NFkappaB target gene, providing a direct link between NFkappaB activity and centrosome duplication, with implications for the role of these transcription factors in tumorigenesis. PMID: 23974100
  35. Plk4 dynamically localizes to distinct subcentrosomal regions by interacting with two hierarchically regulated scaffolds, Cep192 and Cep152. PMID: 24277814
  36. Studies indicate that autophosphorylation of Nek7 and Plk4 occurred through an intermolecular mechanism, the kinases Aurora-A and Chk2 followed an intramolecular mechanism. PMID: 23821772
  37. cooperation between Cep192 and Cep152 is crucial for centriole recruitment of Plk4 and centriole duplication during the cell cycle. PMID: 23641073
  38. If both p53 and the SAPKK MKK4 are simultaneously inactivated, persistent polo-like kinase 4 activity combined with the lack of SAPK-mediated inhibition of centrosome duplication conspire to induce supernumerary centrosomes under stress. PMID: 23653187
  39. Preventing Plk4 autoregulation causes centrosome amplification, stabilization of p53, and loss of cell proliferation PMID: 23249732
  40. CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer. PMID: 23019411
  41. Study demonstrated that PLK4 was remarkably downregulated in HCC and could be served as a potential prognostic marker for patients with this deadly disease. PMID: 22829937
  42. STIL cooperates with SAS-6 and PLK4 in the control of centriole number and represents a key centriole duplication factor in human cells. PMID: 22349698
  43. Plk4 is a centriole-localized kinase that does not directly regulate cytokinesis. PMID: 22456511
  44. The activity of SCF-FBXW5 is negatively regulated by Polo-like kinase 4 (PLK4), which phosphorylates FBXW5 at Ser 151 to suppress its ability to ubiquitylate HsSAS-6. PMID: 21725316
  45. These results highlight the critical role of PLK4 transcriptional deregulation in centriole multiplication in HPV-16 E7-expressing cells. PMID: 21609466
  46. CDK11(p58), which accumulates only in the vicinity of mitotic centrosomes, directly interacts with the centriole-associated protein kinase Plk4 that regulates centriole number in cells. PMID: 21297952
  47. Results suggest that Cep152 recruits Plk4 and CPAP to the centrosome to ensure a faithful centrosome duplication process. PMID: 21059844
  48. Data show that Cep152 can be phosphorylated by Plk4 in vitro, suggesting that Cep152 acts with Plk4 to initiate centriole formation. PMID: 21059850
  49. Data suggest that active Plk4 promotes its own degradation by catalyzing betaTrCP binding through trans-autophosphorylation (phosphorylation by the other kinase in the dimer) within homodimers. PMID: 20516151
  50. Data suggest that polo-like kinase 4 activity is restricted to the centrosome to prevent aberrant centriole assembly and sustained kinase activity is required for centriole duplication. PMID: 20032307

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Involvement in disease
Microcephaly and chorioretinopathy, autosomal recessive, 2 (MCCRP2)
Subcellular Location
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus, nucleolus. Cleavage furrow. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Associates with centrioles throughout the cell cycle. According to PubMed:16244668, it is not present at cleavage furrows.
Protein Families
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
Database Links

HGNC: 11397

OMIM: 605031

KEGG: hsa:10733

STRING: 9606.ENSP00000270861

UniGene: Hs.172052

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