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Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1)

 PLK1_RAT                Reviewed;         603 AA.
Q62673; F1LNH6; Q5XHX4;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 2.
23-MAY-2018, entry version 159.
RecName: Full=Serine/threonine-protein kinase PLK1;
EC=2.7.11.21;
AltName: Full=Polo-like kinase 1;
Short=PLK-1;
Name=Plk1; Synonyms=Plk;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
Amstrup J., Hansen J.A., Hxirlis Nielsen J.;
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- 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 (By
similarity). {ECO:0000250|UniProtKB:P53350,
ECO:0000250|UniProtKB:Q07832}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P53350}.
-!- ENZYME REGULATION: Activated by phosphorylation of Thr-210 by
AURKA; phosphorylation by AURKA is enhanced by BORA. Once
activated, activity is stimulated by binding target proteins.
Binding of target proteins has no effect on the non-activated
kinase. Several inhibitors targeting PLKs are currently in
development and are under investigation in a growing number of
clinical trials, such as BI 2536, an ATP-competitive PLK1
inhibitor or BI 6727, a dihydropteridinone that specifically
inhibits the catalytic activity of PLK1 (By similarity).
{ECO:0000250|UniProtKB:P53350}.
-!- SUBUNIT: Interacts with CEP170 and EVI5. Interacts and
phosphorylates ERCC6L. Interacts with FAM29A. Interacts with
SLX4/BTBD12 and TTDN1. Interacts with BUB1B. Interacts (via POLO-
box domain) with the phosphorylated form of BUB1, CENPU and
CDC25C. Interacts with isoform 3 of SGO1. Interacts with BORA,
KIF2A and AURKA. Interacts with TOPORS and CYLD. Interacts with
ECT2; the interaction is stimulated upon phosphorylation of ECT2
on 'Thr-444'. Interacts with PRC1. Interacts with KIF20A/MKLP2
(when phosphorylated), leading to the recruitment at the central
spindle. Interacts (via POLO box domains) with PPP1R12A/MYPT1
(when previously phosphorylated by CDK1). Part of an astrin
(SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1,
DYNLL1 and SGO2. Interacts with BIRC6/bruce. Interacts with CDK1-
phosphorylated FRY; this interaction occurs in mitotic cells, but
not in interphase cells. FRY interaction facilitates AURKA-
mediated PLK1 phosphorylation. Interacts with CDK1-phosphorylated
DCTN6 during mitotic prometaphase; the interaction facilitates
recruitment to kinetochores. Interacts with CEP68; the interaction
phosphorylates CEP68. Interacts (via POLO-box domain) with DCTN1.
Interacts with FOPNL in later G1, S, G2 and M phases of the cell
cycle; this interaction recruits PLK1 to centrosomes, a step
required for S phase progression. Interacts with HSF1; this
interaction increases upon heat shock but does not modulate
neither HSF1 homotrimerization nor DNA-binding activities.
Interacts with HNRNPU; this interaction induces phosphorylation of
HNRNPU in mitosis. Interacts (via its N-terminus) with RIOK2 (By
similarity). {ECO:0000250|UniProtKB:P53350}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53350}.
Chromosome, centromere, kinetochore
{ECO:0000250|UniProtKB:P53350}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P53350}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:P53350}. Midbody
{ECO:0000250|UniProtKB:P53350}. Note=localization at the
centrosome starts at the G1/S transition (By similarity). During
early stages of mitosis, the phosphorylated form is detected on
centrosomes and kinetochores. Localizes to the outer kinetochore.
Presence of SGO1 and interaction with the phosphorylated form of
BUB1 is required for the kinetochore localization. Localizes onto
the central spindle by phosphorylating and docking at midzone
proteins KIF20A/MKLP2 and PRC1 (By similarity). Colocalizes with
FRY to separating centrosomes and spindle poles from prophase to
metaphase in mitosis, but not in other stages of the cell cycle
(By similarity). Localization to the centrosome is required for S
phase progression (By similarity). Colocalizes with HSF1 at the
spindle poles during prometaphase (By similarity).
{ECO:0000250|UniProtKB:P53350}.
-!- DOMAIN: The POLO box domains act as phosphopeptide-binding module
that recognize and bind serine-[phosphothreonine/phosphoserine]-
(proline/X) motifs. PLK1 recognizes and binds docking proteins
that are already phosphorylated on these motifs, and then
phosphorylates them. PLK1 can also create its own docking sites by
mediating phosphorylation of serine-
[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently
recognized by the POLO box domains (By similarity).
{ECO:0000250|UniProtKB:P53350}.
-!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-210.
Phosphorylation at Thr-210 is first detected on centrosomes in the
G2 phase of the cell cycle, peaks in prometaphase and gradually
disappears from centrosomes during anaphase. Dephosphorylation at
Thr-210 at centrosomes is probably mediated by protein phosphatase
1C (PP1C), via interaction with PPP1R12A/MYPT1.
Autophosphorylation and phosphorylation of Ser-137 may not be
significant for the activation of PLK1 during mitosis, but may
enhance catalytic activity during recovery after DNA damage
checkpoint. Phosphorylated in vitro by STK10 (By similarity).
{ECO:0000250|UniProtKB:P53350}.
-!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome
(APC/C) in anaphase and following DNA damage, leading to its
degradation by the proteasome. Ubiquitination is mediated via its
interaction with FZR1/CDH1. Ubiquitination and subsequent
degradation prevents entry into mitosis and is essential to
maintain an efficient G2 DNA damage checkpoint. Monoubiquitination
at Lys-492 by the BCR(KLHL22) ubiquitin ligase complex does not
lead to degradation: it promotes PLK1 dissociation from
phosphoreceptor proteins and subsequent removal from kinetochores,
allowing silencing of the spindle assembly checkpoint (SAC) and
chromosome segregation (By similarity).
{ECO:0000250|UniProtKB:P53350}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U10188; AAA18885.1; -; mRNA.
EMBL; BC083926; AAH83926.1; -; mRNA.
RefSeq; NP_058796.1; NM_017100.1.
UniGene; Rn.11034; -.
SMR; Q62673; -.
STRING; 10116.ENSRNOP00000025629; -.
iPTMnet; Q62673; -.
PhosphoSitePlus; Q62673; -.
PaxDb; Q62673; -.
PRIDE; Q62673; -.
GeneID; 25515; -.
KEGG; rno:25515; -.
UCSC; RGD:3352; rat.
CTD; 5347; -.
RGD; 3352; Plk1.
eggNOG; KOG0575; Eukaryota.
eggNOG; ENOG410XQBP; LUCA.
HOGENOM; HOG000248546; -.
HOVERGEN; HBG001843; -.
InParanoid; Q62673; -.
KO; K06631; -.
BRENDA; 2.7.11.21; 5301.
PRO; PR:Q62673; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0051233; C:spindle midzone; IDA:RGD.
GO; GO:0000922; C:spindle pole; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0051081; P:nuclear envelope disassembly; ISS:UniProtKB.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:RGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
GO; GO:0090435; P:protein localization to nuclear envelope; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; ISS:UniProtKB.
CDD; cd13118; POLO_box_1; 1.
CDD; cd13117; POLO_box_2; 1.
CDD; cd14187; STKc_PLK1; 1.
Gene3D; 3.30.1120.30; -; 3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033702; PLK1_cat.
InterPro; IPR033701; POLO_box_1.
InterPro; IPR033695; POLO_box_2.
InterPro; IPR000959; POLO_box_dom.
InterPro; IPR036947; POLO_box_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00659; POLO_box; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50078; POLO_BOX; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase;
Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN 1 603 Serine/threonine-protein kinase PLK1.
/FTId=PRO_0000086558.
DOMAIN 53 305 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 417 480 POLO box 1. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
DOMAIN 515 584 POLO box 2. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 59 67 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 178 181 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 194 221 Activation loop. {ECO:0000250}.
REGION 493 507 Linker. {ECO:0000250}.
REGION 538 540 Important for interaction with
phosphorylated proteins. {ECO:0000250}.
MOTIF 337 340 D-box that targets the protein for
proteasomal degradation in anaphase.
{ECO:0000250}.
ACT_SITE 176 176 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 82 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 131 131 ATP; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
BINDING 194 194 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 210 210 Phosphothreonine; by AURKA.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 214 214 Phosphothreonine.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 269 269 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 335 335 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:P53350}.
MOD_RES 498 498 Phosphothreonine.
{ECO:0000250|UniProtKB:P53350}.
CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P53350}.
CROSSLNK 338 338 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P53350}.
CROSSLNK 492 492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P53350}.
CONFLICT 27 27 A -> V (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 32 32 G -> V (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 45 45 M -> V (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 51 51 R -> Q (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 80 80 P -> A (in Ref. 2; AAH83926).
{ECO:0000305}.
CONFLICT 102 102 I -> T (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 109 109 A -> E (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 291 291 T -> A (in Ref. 1; AAA18885).
{ECO:0000305}.
CONFLICT 543 544 LC -> RG (in Ref. 1; AAA18885).
{ECO:0000305}.
SEQUENCE 603 AA; 68291 MW; D756DD742CB14F6E CRC64;
MNAAAKAGKL ARAPADLGKG GVPGDAAPGA PGAAPLAKEI PEVLMDPRSR RQYVRGRFLG
KGGFAKCFEI SDSDTKEVFP GKIVPKSLLL KPHQKEKMSM EISIHRSLAH QHVVGFHGFF
EDSDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN QVIHRDLKLG
NLFLNEDLEV KIGDFGLATK VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGVENP LPDRPREKEE
PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLN
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK
LILCPLMAAV TYINEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSACNRL
KAS


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52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur