Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Separin homolog sep-1 (EC 3.4.22.49) (Separase)

 SEP1_CAEEL              Reviewed;        1262 AA.
G5ED39;
07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
25-OCT-2017, entry version 57.
RecName: Full=Separin homolog sep-1 {ECO:0000305};
EC=3.4.22.49 {ECO:0000305|PubMed:25919583};
AltName: Full=Separase {ECO:0000312|WormBase:Y47G6A.12};
Name=sep-1 {ECO:0000312|WormBase:Y47G6A.12};
ORFNames=Y47G6A.12 {ECO:0000312|WormBase:Y47G6A.12};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:AAK77200.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF CYS-450.
PubMed=11728305; DOI=10.1016/S0960-9822(01)00588-7;
Siomos M.F., Badrinath A., Pasierbek P., Livingstone D., White J.,
Glotzer M., Nasmyth K.;
"Separase is required for chromosome segregation during meiosis I in
Caenorhabditis elegans.";
Curr. Biol. 11:1825-1835(2001).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, INTERACTION WITH IFY-1, AND DISRUPTION PHENOTYPE.
PubMed=12498686;
Kitagawa R., Law E., Tang L., Rose A.M.;
"The Cdc20 homolog, FZY-1, and its interacting protein, IFY-1, are
required for proper chromosome segregation in Caenorhabditis
elegans.";
Curr. Biol. 12:2118-2123(2002).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11832245; DOI=10.1016/S1534-5807(02)00114-4;
Rappleye C.A., Tagawa A., Lyczak R., Bowerman B., Aroian R.V.;
"The anaphase-promoting complex and separin are required for embryonic
anterior-posterior axis formation.";
Dev. Cell 2:195-206(2002).
[5] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-450.
PubMed=17913784; DOI=10.1242/dev.011361;
Bembenek J.N., Richie C.T., Squirrell J.M., Campbell J.M.,
Eliceiri K.W., Poteryaev D., Spang A., Golden A., White J.G.;
"Cortical granule exocytosis in C. elegans is regulated by cell cycle
components including separase.";
Development 134:3837-3848(2007).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF CYS-450 AND CYS-1040.
PubMed=20116245; DOI=10.1016/j.cub.2009.12.045;
Bembenek J.N., White J.G., Zheng Y.;
"A role for separase in the regulation of RAB-11-positive vesicles at
the cleavage furrow and midbody.";
Curr. Biol. 20:259-264(2010).
[7] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF CYS-232 AND LEU-556.
PubMed=21878498; DOI=10.1242/jcs.073379;
Richie C.T., Bembenek J.N., Chestnut B., Furuta T., Schumacher J.M.,
Wallenfang M., Golden A.;
"Protein phosphatase 5 is a negative regulator of separase function
during cortical granule exocytosis in C. elegans.";
J. Cell Sci. 124:2903-2913(2011).
[8] {ECO:0000305}
ENZYME REGULATION, INTERACTION WITH IFY-1, AND DISRUPTION PHENOTYPE.
PubMed=23578927; DOI=10.1242/dev.090688;
Wang R., Kaul Z., Ambardekar C., Yamamoto T.G., Kavdia K., Kodali K.,
High A.A., Kitagawa R.;
"HECT-E3 ligase ETC-1 regulates securin and cyclin B1 cytoplasmic
abundance to promote timely anaphase during meiosis in C. elegans.";
Development 140:2149-2159(2013).
[9] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
CYS-450.
PubMed=23401519; DOI=10.1073/pnas.1213888110;
Schvarzstein M., Pattabiraman D., Bembenek J.N., Villeneuve A.M.;
"Meiotic HORMA domain proteins prevent untimely centriole
disengagement during Caenorhabditis elegans spermatocyte meiosis.";
Proc. Natl. Acad. Sci. U.S.A. 110:E898-E907(2013).
[10] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=25919583; DOI=10.1371/journal.pone.0125382;
Monen J., Hattersley N., Muroyama A., Stevens D., Oegema K., Desai A.;
"Separase Cleaves the N-Tail of the CENP-A Related Protein CPAR-1 at
the Meiosis I Metaphase-Anaphase Transition in C. elegans.";
PLoS ONE 10:E0125382-E0125382(2015).
[11] {ECO:0000305}
STRUCTURE BY ELECTRON MICROSCOPY (24 ANGSTROMS) IN COMPLEX WITH IFY-1,
AND ENZYME REGULATION.
PubMed=27249343; DOI=10.1098/rsob.160032;
Bachmann G., Richards M.W., Winter A., Beuron F., Morris E.,
Bayliss R.;
"A closed conformation of the Caenorhabditis elegans separase-securin
complex.";
Open Biol. 6:160032-160032(2016).
[12] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH IFY-1, AND
ENZYME REGULATION.
PubMed=28263324; DOI=10.1038/nsmb.3386;
Boland A., Martin T.G., Zhang Z., Yang J., Bai X.C., Chang L.,
Scheres S.H., Barford D.;
"Cryo-EM structure of a metazoan separase-securin complex at near-
atomic resolution.";
Nat. Struct. Mol. Biol. 24:414-418(2017).
-!- FUNCTION: Cysteine protease, which plays a central role in
homologous chromosome separation during meiosis I and in sister
chromatid separation during embryonic mitosis (PubMed:11728305,
PubMed:12498686, PubMed:20116245, PubMed:21878498). Promotes
chromosome/sister chromatid segregation by cleaving the scc-1
(mitosis) and rec-8 (meiosis) subunits of the cohesin complex at
the onset of anaphase (Probable). May cleave histone H3-like
protein cpar-1 during meiosis I metaphase-anaphase transition
(PubMed:25919583). Promotes cortical granule exocytosis after
oocyte fertilization during the first meiotic anaphase
(PubMed:17913784, PubMed:21878498). Essential for embryonic
cytokinesis by regulating rab-11-positive vesicle trafficking at
the plasma membrane at the cleavage furrow and midbody
(PubMed:20116245). Regulates centriole segregation during
spermatocyte meiosis (PubMed:23401519). Required for embryonic
anterior-posterior axis formation (PubMed:11832245).
{ECO:0000269|PubMed:11728305, ECO:0000269|PubMed:11832245,
ECO:0000269|PubMed:12498686, ECO:0000269|PubMed:17913784,
ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21878498,
ECO:0000269|PubMed:23401519, ECO:0000269|PubMed:25919583,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: All bonds known to be hydrolyzed by this
endopeptidase have arginine in P1 and an acidic residue in P4. P6
is often occupied by an acidic residue or by a hydroxy-amino-acid
residue, the phosphorylation of which enhances cleavage.
{ECO:0000305|PubMed:25919583}.
-!- ENZYME REGULATION: Probably maintained in an inactive state via
its interaction with securin ify-1 which acts as a pseudosubstrate
thereby blocking access to the catalytic site. Upon ify-1
degradation at the onset of anaphase, sep-1 is likely to become
active. In addition, interaction with ify-1 stabilizes sep-1.
{ECO:0000305|PubMed:23578927, ECO:0000305|PubMed:27249343,
ECO:0000305|PubMed:28263324}.
-!- SUBUNIT: Forms a complex with securin-like protein ify-1 (via C-
terminus) (PubMed:12498686, PubMed:23578927, PubMed:27249343,
PubMed:28263324). Interaction with ify-1 stabilizes sep-1
(PubMed:27249343, PubMed:28263324). Also maintains the complex in
the cytoplasm during interphase and recruits it to chromosomes
during the first meiotic division (PubMed:23578927).
{ECO:0000269|PubMed:12498686, ECO:0000269|PubMed:23578927,
ECO:0000269|PubMed:27249343, ECO:0000269|PubMed:28263324}.
-!- INTERACTION:
Q18235:ify-1; NbExp=3; IntAct=EBI-326265, EBI-331643;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17913784,
ECO:0000269|PubMed:23401519}. Chromosome
{ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245,
ECO:0000269|PubMed:23401519}. Cytoplasmic granule
{ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:21878498}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17913784}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245,
ECO:0000269|PubMed:23401519}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245,
ECO:0000269|PubMed:21878498}. Cleavage furrow
{ECO:0000269|PubMed:20116245}. Midbody
{ECO:0000269|PubMed:20116245}. Note=Before ovulation, accumulates
on chromosomes and cortical filaments in oocytes
(PubMed:17913784). By metaphase I, dissociates from filaments and
transiently localizes to cortical granules until their exocytosis
during anaphase I followed by an accumulation at the cortex near
the polar body (PubMed:17913784). Localizes to meiotic spindle
matrix (PubMed:21878498). During mitotic metaphase and anaphase,
localizes to chromosomes, centrosomes and the spindle matrix
(PubMed:17913784, PubMed:20116245, PubMed:21878498). During
spermatogenesis, localizes to the spermatocyte cytoplasm
throughout meiotic prophase I (PubMed:23401519). At the diplotene
stage of prophase I accumulates at low levels in puncta around the
nuclear envelope (PubMed:23401519). At diakinesis, transiently
localizes to centrosomes until nuclear envelope breakdown
(PubMed:23401519). At metaphase I and II becomes highly enriched
around chromosomes (PubMed:23401519). At anaphase I and II,
chromosomal localization is reduced and centrosome localization is
highly increased (PubMed:23401519). Localizes to residual body
during the budding division leading to spermatid formation
(PubMed:23401519). {ECO:0000269|PubMed:17913784,
ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21878498,
ECO:0000269|PubMed:23401519}.
-!- TISSUE SPECIFICITY: Expressed in oocytes (PubMed:17913784).
Expressed in male germline (PubMed:23401519). Expressed in
spermatocytes but undetectable in spermatids (at protein level)
(PubMed:23401519). {ECO:0000269|PubMed:17913784,
ECO:0000269|PubMed:23401519}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
{ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:20116245}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
lethality where embryos are arrested at the onset of meiotic
anaphase I (PubMed:11728305, PubMed:12498686, PubMed:23578927).
During the first meiotic cell division, homologous chromosome
segregation and formation of polar bodies are impaired, and
multiple centrosomes accumulate resulting from a failure to
undergo cytokinesis (PubMed:11728305, PubMed:12498686,
PubMed:17913784, PubMed:20116245, PubMed:21878498). During meiotic
anaphase I, impaired cortical granules exocytosis resulting in the
formation of a one-layered eggshell instead of the normal three-
layered eggshell (PubMed:11728305, PubMed:17913784,
PubMed:21878498). In oocytes, ify-1 prematurely enters the nucleus
prior to the nuclear envelope breakdown and fails to associate
with chromosomes during meiosis I without affecting its spindle
association (PubMed:23578927). Prevents histone H3-like cpar-1
cleavage at the onset of meiotic anaphase I and during embryonic
mitosis (PubMed:25919583). In addition, in the one-cell embryo,
causes defects in embryonic anterior-posterior polarization
characterized by a failure of cortical association and posterior
positioning of the paternal pronucleus and the mislocalization of
par-2 and pie-1 (PubMed:11832245). During the first embryonic
mitosis, abnormal accumulation of rab-11 at the cleavage furrow
and midbody and furrow regression resulting in a failure to
complete cytokinesis (PubMed:20116245).
{ECO:0000269|PubMed:11728305, ECO:0000269|PubMed:11832245,
ECO:0000269|PubMed:12498686, ECO:0000269|PubMed:17913784,
ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21878498,
ECO:0000269|PubMed:23578927, ECO:0000269|PubMed:25919583}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF399825; AAK77200.1; -; mRNA.
EMBL; BX284601; CCD72557.1; -; Genomic_DNA.
RefSeq; NP_491160.1; NM_058759.3.
UniGene; Cel.17513; -.
PDB; 5MZ6; EM; 3.80 A; 1=1-1262.
PDBsum; 5MZ6; -.
SMR; G5ED39; -.
IntAct; G5ED39; 3.
STRING; 6239.Y47G6A.12; -.
MEROPS; C50.004; -.
EPD; G5ED39; -.
EnsemblMetazoa; Y47G6A.12; Y47G6A.12; WBGene00004775.
GeneID; 171912; -.
KEGG; cel:CELE_Y47G6A.12; -.
CTD; 171912; -.
WormBase; Y47G6A.12; CE22098; WBGene00004775; sep-1.
eggNOG; KOG1849; Eukaryota.
eggNOG; COG5155; LUCA.
GeneTree; ENSGT00390000004990; -.
KO; K02365; -.
OMA; MHEARSK; -.
OrthoDB; EOG091G03VI; -.
Reactome; R-CEL-2467813; Separation of Sister Chromatids.
PRO; PR:G5ED39; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00004775; -.
GO; GO:0005938; C:cell cortex; IDA:WormBase.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:WormBase.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
GO; GO:0060473; C:cortical granule; IDA:WormBase.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0072687; C:meiotic spindle; IDA:WormBase.
GO; GO:0070090; C:metaphase plate; IDA:WormBase.
GO; GO:0030496; C:midbody; IDA:WormBase.
GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:WormBase.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:WormBase.
GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB.
GO; GO:0060471; P:cortical granule exocytosis; IMP:WormBase.
GO; GO:0030703; P:eggshell formation; IMP:UniProtKB.
GO; GO:0051307; P:meiotic chromosome separation; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0051306; P:mitotic sister chromatid separation; IMP:UniProtKB.
GO; GO:0048609; P:multicellular organismal reproductive process; IMP:WormBase.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:UniProtKB.
GO; GO:0016485; P:protein processing; IMP:UniProtKB.
GO; GO:0030997; P:regulation of centriole-centriole cohesion; IMP:UniProtKB.
GO; GO:0017157; P:regulation of exocytosis; IMP:UniProtKB.
GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
GO; GO:0061062; P:regulation of nematode larval development; IMP:WormBase.
InterPro; IPR005314; Peptidase_C50.
InterPro; IPR030397; SEPARIN_core_dom.
PANTHER; PTHR12792; PTHR12792; 2.
PROSITE; PS51700; SEPARIN; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Chromosome;
Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton;
Hydrolase; Meiosis; Mitosis; Protease; Reference proteome;
Thiol protease.
CHAIN 1 1262 Separin homolog sep-1. {ECO:0000305}.
/FTId=PRO_0000440177.
DOMAIN 957 1051 Peptidase C50. {ECO:0000255|PROSITE-
ProRule:PRU01037}.
ACT_SITE 1040 1040 {ECO:0000255|PROSITE-ProRule:PRU01037}.
MUTAGEN 232 232 C->Y: In ax521; embryos are arrested at
the one-cell stage. No extrusion of polar
bodies. Multiple rounds of DNA
replication occur without cytokinesis.
Slower chromosome segregation during the
first embryonic mitosis but no chromosome
separation defects during meiosis.
Reduced cortical granules exocytosis
during anaphase I resulting in eggshell
defects. Loss of cortical granule
localization.
{ECO:0000269|PubMed:21878498}.
MUTAGEN 450 450 C->Y: In e2406; temperature sensitive
mutant which at the restrictive
temperature of 25 degrees Celsius
displays slow chromosome segregation and
lacks cytokinesis in the one-cell stage
embryo and during meiosis I. Reduced
cortical granules exocytosis during
anaphase I. Loss of cortical granule
localization. Loss of cytokinesis
resulting from furrow regression. At the
end of second meiotic division, causes a
premature dissociation of the two
centrioles in spermatocytes. Permanent
localization to centrosome throughout
meiosis. Abnormal localization to sperm
DNA in to a foci near the sperm chromatin
in fertilized embryos.
{ECO:0000269|PubMed:11728305,
ECO:0000269|PubMed:17913784,
ECO:0000269|PubMed:20116245,
ECO:0000269|PubMed:23401519}.
MUTAGEN 556 556 L->F: In ax110; embryos are arrested at
the one-cell stage. No extrusion of polar
bodies. Multiple rounds of DNA
replication occur without cytokinesis.
Slower chromosome segregation during the
first embryonic mitosis but no chromosome
separation defects during meiosis.
Reduced cortical granules exocytosis
during anaphase I resulting in eggshell
defects. Loss of meiotic spindle and
cortical granule localization. In a php-5
(av101) mutant background, cortical
granule exocytosis and chromosome
segregation are normal.
{ECO:0000269|PubMed:21878498}.
MUTAGEN 1040 1040 C->S: Probable loss of catalytic
activity. Stronger accumulation at
chromosomes, centrosomes, spindle,
cleavage furrow and midbody during the
first embryonic mitosis.
{ECO:0000269|PubMed:20116245}.
SEQUENCE 1262 AA; 144121 MW; 4CBAAB9E0330CEB3 CRC64;
MKITNKSVDK QHIEKLDELR KNVSCTVIGF AEQTAELQQE ISELFIAEFG VNGPIDMNSL
SKLARITSYY ASSEYFQGLA KYQRTACKMF ITWQTLRKEA MECRSKDREI FASIPAKLCF
FYFYNGELCR AVVCLLDYID LSDDTLAKEA ALRWLMFLGE TELIEKKLKT WKMDKSSKDM
FSATEFAMNY LKKSEYRVEM LEKLMKLRDK VKSDPTRSFS RYELASYVSW LCSTLSNVPV
GSALRECEFP DRVSHIQEAA LKSDSLVRNR IPGLASSQFD NSVNASIWPF LDGHQEDSNY
YVHIGSTIAW HFEMRRECAL VNVTTAQTRD SMSAMILNLR VALKSASFFR VLQTTNTLAY
YSSIIEEAGS EKNAKLMRVS CVNLLSSNPI IVRCSTPKET GATSRAHTPM AGSSVSEKQN
TMRPDLADLL GDLELLDEQS FHPITRSCVC NVCTIYPLHS SFAAEYMMSY AIHSDFSQLS
IKHFNDEFAR IRERGMSSQV LMHRDSSVRP RPNIIQNEIF GMCVIRWLTK KLDSKESADE
DTMEIFNNAL KIVRYLQQRT TDMILAVTQL GRQLEFPMEC NYSWMRPTIR KPRVKATIDC
AVDILRAVSP FGRRPKVEKL EKNLQPFDKE RFEKVRLAMR NEMNHYGHIL YREWRCRLFA
YVGRTSRDPW EAAYAWAEST QIGARNAVQS RLEKCKRGLV TMSGHDRFKT CVQSMPDEMT
LVQIAMADDK TIYLVKLHAD RDPIIMPLAH YSQAVELMDK FTFLLDEDEM IAKYPGDITP
EEFWKRRKIV DGRMMTFVDE VQKHFLGVAA SLLMPSGQLG PKAAELAIKI HKLSKGGLLL
GEAKEMVYQS KLMDAKSWEA LILRFCEMRT TDEKFKSFLP LMHRNSVEVM NQDDSIVTEK
KYTYLVICPH LSQFCWERLP IFDEYPYVGR QVSIHSTFSQ LEAMKSQEKQ IPLQIDVQNA
YYILDPDNNL GETQKRMVEY INKFNWEGTV GSAPKSNEIS AALSQRDAFF FIGHGSGSSV
MPRSVLKQST CNAISLLMGC GSVRTIPQAL GFDGKTAILD YAMAKCPLIV GCLWTVTDGE
IDRFLIRMID DCFEDSKSLT GIDKLRQLSE AMHEARSKAR LKYLTGAAVV MYGLPVVAKQ
TTPFVEKDQR NLPQTPKTSA RTSMRMETVP KTPKQEFVTS KSVPMTPIFS NNENKSPSRA
RMPSRVLKTP RQVKTFQEED DEAPKRSTTR QLKPLVAPPI PATPTTRTTR SSARTPSRSR
NL


Related products :

Catalog number Product name Quantity
EIAAB13323 Caspase-like protein ESPL1,Esp1,Espl1,Extra spindle poles-like 1 protein,Kiaa0165,Mouse,Mus musculus,Separase,Separin
EIAAB13324 Caspase-like protein ESPL1,ESP1,ESPL1,Extra spindle poles-like 1 protein,Homo sapiens,Human,KIAA0165,Separase,Separin
28-866 PTTG1 is a homolog of yeast securing proteins, which prevent separins from promoting sister chromatid separation. It is an anaphase-promoting complex (APC) substrate that associates with a separin unt 0.1 mg
orb96466 Separase antibody 50 ug
orb100438 Separase antibody 100 ug
orb100438 Separase antibody 200 ug
YF-MA11199 anti-Separase (6H6) 100 ug
YF-PA25396 anti-Separase 50 ul
orb103466 Separase antibody (FITC) 100 ug
BP302-214 Separase Blocking Peptide 50 ug
A023679 Rabbit Anti-Separase Ab 100ul
BP302-215 Separase Blocking Peptide 50 ug
AP20283PU-N Separin _ ESPL1 100 µg
NB100-439 Separin _ ESPL1 0.1 ml
NB100-439 Separin _ ESPL1 0.1 ml
GTX16170 Separin _ ESPL1 100 µl
GTX15955 Separin _ ESPL1 100 µl
GTX15955 Separin _ ESPL1 100 µl
GTX16170 Separin _ ESPL1 100 µl
NB100-330 Separin _ ESPL1 0.1 ml
NB100-330 Separin _ ESPL1 0.1 ml
SP2070a Separase-S801 Phospho Peptide
SP2071a Separase-S1176 Phospho Peptide
SP2069a Separase-S748 Phospho Peptide
BC110-55295 Separin _ ESPL1 0.1 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
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