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

Heat shock protein 90-2 (AtHSP90.2) (AtHsp90-2) (Heat shock protein 81-2) (Hsp81-2) (Protein EARLY-RESPONSIVE TO DEHYDRATION 8) (Protein LOSS OF RECOGNITION OF AVRRPM1 2) (Protein MUTANT SNC1-ENHANCING 12)

 HS902_ARATH             Reviewed;         699 AA.
P55737; Q8H158;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 152.
RecName: Full=Heat shock protein 90-2 {ECO:0000305};
Short=AtHSP90.2 {ECO:0000305};
Short=AtHsp90-2 {ECO:0000303|PubMed:11599565};
AltName: Full=Heat shock protein 81-2 {ECO:0000305};
Short=Hsp81-2 {ECO:0000303|PubMed:11599565};
AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION 8;
AltName: Full=Protein LOSS OF RECOGNITION OF AVRRPM1 2;
AltName: Full=Protein MUTANT SNC1-ENHANCING 12 {ECO:0000303|PubMed:24889324};
Name=HSP90-2 {ECO:0000303|PubMed:11599565};
Synonyms=ERD8, HSP81-2 {ECO:0000303|PubMed:11599565}, LRA2,
MUSE12 {ECO:0000303|PubMed:24889324}; OrderedLocusNames=At5g56030;
ORFNames=MDA7.7;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=16668895; DOI=10.1104/pp.99.2.383;
Takahashi T., Naito S., Komeda Y.;
"Isolation and analysis of the expression of two genes for the 81-
kilodalton heat-shock proteins from Arabidopsis.";
Plant Physiol. 99:383-390(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:THFOPI>2.0.CO;2;
Krishna P., Gloor G.;
"The Hsp90 family of proteins in Arabidopsis thaliana.";
Cell Stress Chaperones 6:238-246(2001).
[6]
FUNCTION, INTERACTION WITH RPM1; RAR1 AND SGT1B, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF ASP-80; GLY-95 AND SER-100.
PubMed=14592967; DOI=10.1093/emboj/cdg547;
Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A.,
Shirasu K., Dangl J.L.;
"Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1
disease resistance protein.";
EMBO J. 22:5679-5689(2003).
[7]
FUNCTION, AND INTERACTION WITH HSFA1D.
PubMed=17965410; DOI=10.1074/jbc.M707168200;
Yamada K., Fukao Y., Hayashi M., Fukazawa M., Suzuki I., Nishimura M.;
"Cytosolic HSP90 regulates the heat shock response that is responsible
for heat acclimation in Arabidopsis thaliana.";
J. Biol. Chem. 282:37794-37804(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[9]
FUNCTION, INTERACTION WITH RAR1 AND SGT1B, AND MUTAGENESIS OF ALA-11;
ALA-42 AND ARG-337.
PubMed=19487680; DOI=10.1073/pnas.0904877106;
Hubert D.A., He Y., McNulty B.C., Tornero P., Dangl J.L.;
"Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone
function in plant NB-LRR disease resistance protein regulation.";
Proc. Natl. Acad. Sci. U.S.A. 106:9556-9563(2009).
[10]
FUNCTION.
PubMed=20147301; DOI=10.1093/pcp/pcq015;
Nishizawa-Yokoi A., Tainaka H., Yoshida E., Tamoi M., Yabuta Y.,
Shigeoka S.;
"The 26S proteasome function and Hsp90 activity involved in the
regulation of HsfA2 expression in response to oxidative stress.";
Plant Cell Physiol. 51:486-496(2010).
[11]
FUNCTION.
PubMed=21586649; DOI=10.1104/pp.111.174425;
Clement M., Leonhardt N., Droillard M.J., Reiter I., Montillet J.L.,
Genty B., Lauriere C., Nussaume L., Noel L.D.;
"The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are
important for stomatal closure and modulate abscisic acid-dependent
physiological responses in Arabidopsis.";
Plant Physiol. 156:1481-1492(2011).
[12]
HOMODIMERIZATION, AND INTERACTION WITH OEP61; OEP64 AND OM64.
PubMed=24036116; DOI=10.1074/jbc.M113.493015;
Schweiger R., Soll J., Jung K., Heermann R., Schwenkert S.;
"Quantification of interaction strengths between chaperones and
tetratricopeptide repeat domain-containing membrane proteins.";
J. Biol. Chem. 288:30614-30625(2013).
[13]
FUNCTION.
PubMed=24611624; DOI=10.1111/nph.12760;
Bao F., Huang X., Zhu C., Zhang X., Li X., Yang S.;
"Arabidopsis HSP90 protein modulates RPP4-mediated temperature-
dependent cell death and defense responses.";
New Phytol. 202:1320-1334(2014).
[14]
FUNCTION, AND MUTAGENESIS OF ARG-33 AND ASP-41.
PubMed=24889324; DOI=10.1111/tpj.12573;
Huang S., Monaghan J., Zhong X., Lin L., Sun T., Dong O.X., Li X.;
"HSP90s are required for NLR immune receptor accumulation in
Arabidopsis.";
Plant J. 79:427-439(2014).
-!- FUNCTION: Molecular chaperone. Involved in RPM1-mediated
resistance. Component of the RPM1/RAR1/SGT1 complex. May stabilize
RPM1 and protect it from SGT1-mediated degradation. Associates
with RAR1 which may function as co-chaperone. Possesses ATPase
activity (PubMed:14592967, PubMed:19487680). In the absence of
heat shock, negatively regulates heat-inducible genes by actively
suppressing heat shock transcription factor A1D (HSFA1D) function
(PubMed:17965410). Involved in the induction of heat shock
transcription factor A2 (HSFA2) expression in response to
oxidative stress (PubMed:20147301). Required for stomatal closure
and modulates transcriptional and physiological responses to
abscisic acid (ABA) (PubMed:21586649). Regulates RPP4-mediated
temperature-dependent cell death and defense responses
(PubMed:24611624). May assist SGT1B in the formation of SCF E3
ubiquitin ligase complexes that target the immune receptors SNC1,
RPS2 and RPS4 for degradation, to regulate receptor levels and
avoid autoimmunity (PubMed:24889324).
{ECO:0000269|PubMed:14592967, ECO:0000269|PubMed:17965410,
ECO:0000269|PubMed:19487680, ECO:0000269|PubMed:20147301,
ECO:0000269|PubMed:21586649, ECO:0000269|PubMed:24611624,
ECO:0000269|PubMed:24889324}.
-!- SUBUNIT: Homodimer (PubMed:19487680, PubMed:24036116). Interacts
with RPM1, RAR1 and SGT1B (PubMed:14592967, PubMed:19487680).
Interacts with OEP61, OEP64 and OM64 (PubMed:24036116). Interacts
with HSFA1D (PubMed:17965410). {ECO:0000269|PubMed:14592967,
ECO:0000269|PubMed:17965410, ECO:0000269|PubMed:19487680,
ECO:0000269|PubMed:24036116}.
-!- INTERACTION:
P25854:CAM4; NbExp=2; IntAct=EBI-1235834, EBI-1235664;
Q03509:CAM6; NbExp=2; IntAct=EBI-1235834, EBI-1236097;
P59220:CAM7; NbExp=2; IntAct=EBI-1235834, EBI-1236031;
Q9S744:CML9; NbExp=2; IntAct=EBI-1235834, EBI-1236048;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P55737-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Present in all tissues. Most abundantly
expressed in roots followed by floral bud clusters, flowers and
young fruits.
-!- INDUCTION: In contrast to other major heat shock proteins, this
one is also expressed at normal growth temperatures. Levels
increase only slightly after heat shock.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
condition. In case of infection, plants are altered in RPM1-
mediated disease resistance. {ECO:0000269|PubMed:14592967}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB011476; BAB09285.1; -; Genomic_DNA.
EMBL; CP002688; AED96711.1; -; Genomic_DNA.
EMBL; AY062750; AAL32828.1; -; mRNA.
EMBL; AY128805; AAM91205.1; -; mRNA.
EMBL; BT000717; AAN31859.1; -; mRNA.
EMBL; BT001944; AAN71943.1; -; mRNA.
EMBL; BT002535; AAO00895.1; -; mRNA.
RefSeq; NP_200414.1; NM_124985.5. [P55737-1]
UniGene; At.25243; -.
UniGene; At.27546; -.
UniGene; At.45945; -.
ProteinModelPortal; P55737; -.
SMR; P55737; -.
BioGrid; 20945; 16.
DIP; DIP-51470N; -.
IntAct; P55737; 11.
iPTMnet; P55737; -.
SwissPalm; P55737; -.
PRIDE; P55737; -.
EnsemblPlants; AT5G56030.1; AT5G56030.1; AT5G56030. [P55737-1]
GeneID; 835701; -.
Gramene; AT5G56030.1; AT5G56030.1; AT5G56030. [P55737-1]
KEGG; ath:AT5G56030; -.
Araport; AT5G56030; -.
eggNOG; KOG0019; Eukaryota.
eggNOG; COG0326; LUCA.
HOGENOM; HOG000031988; -.
InParanoid; P55737; -.
KO; K04079; -.
PhylomeDB; P55737; -.
Reactome; R-ATH-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-ATH-3371571; HSF1-dependent transactivation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-844456; The NLRP3 inflammasome.
PRO; PR:P55737; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P55737; baseline and differential.
Genevisible; P55737; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0009816; P:defense response to bacterium, incompatible interaction; IMP:UniProtKB.
CDD; cd00075; HATPase_c; 1.
Gene3D; 1.20.120.790; -; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chaperone; Complete proteome;
Cytoplasm; Immunity; Innate immunity; Nucleotide-binding;
Phosphoprotein; Plant defense; Reference proteome; Stress response.
CHAIN 1 699 Heat shock protein 90-2.
/FTId=PRO_0000062947.
NP_BIND 100 101 ATP. {ECO:0000250|UniProtKB:P02829}.
NP_BIND 120 125 ATP. {ECO:0000250|UniProtKB:P02829}.
MOTIF 695 699 TPR repeat-binding.
COMPBIAS 222 226 Poly-Glu.
COMPBIAS 246 252 Poly-Lys.
COMPBIAS 529 532 Poly-Lys.
COMPBIAS 670 673 Poly-Asp.
BINDING 34 34 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 38 38 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 80 80 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 85 85 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 93 93 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 99 99 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 172 172 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 371 371 ATP. {ECO:0000250|UniProtKB:P02829}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:P27323}.
MUTAGEN 11 11 A->T: In hsp90.2-7; No effect on ATPase
activity, dimerization and interaction
with RAR1. Decreased interaction with
SGT1B. {ECO:0000269|PubMed:19487680}.
MUTAGEN 33 33 R->H: In muse12; enhances snc1-mediated
autoimmune phenotypes.
{ECO:0000269|PubMed:24889324}.
MUTAGEN 41 41 D->N: In muse12; enhances snc1-mediated
autoimmune phenotypes.
{ECO:0000269|PubMed:24889324}.
MUTAGEN 42 42 A->T: In hsp90.2-6; Loss of RPM1 function
and accumulation. Loss of ATPase
activity. Loss of dimerization. Loss of
interaction with RAR1 and SGT1B.
{ECO:0000269|PubMed:19487680}.
MUTAGEN 80 80 D->N: In hsp90.2-3/lra2-3; Loss of RPM1
function and accumulation. Loss of ATPase
activity. Loss of dimerization. Loss of
interaction with RAR1 and SGT1B.
{ECO:0000269|PubMed:14592967}.
MUTAGEN 95 95 G->E: In hsp90.2-1/lra2-1; Loss of RPM1
function and accumulation. Loss of ATPase
activity. Loss of dimerization. Loss of
interaction with RAR1 and SGT1B.
{ECO:0000269|PubMed:14592967}.
MUTAGEN 100 100 S->F: In hsp90.2-4/lra2-4; Loss of RPM1
function and accumulation. Loss of ATPase
activity. Loss of dimerization. Normal
interaction with RAR1. Loss of
interaction with SGT1B.
{ECO:0000269|PubMed:14592967}.
MUTAGEN 337 337 R->C: In hsp90.2-6; Decreased
dimerization. Loss of ATPase activity and
interaction with RAR1 and SGT1B.
{ECO:0000269|PubMed:19487680}.
CONFLICT 657 657 S -> N (in Ref. 4; AAN31859).
{ECO:0000305}.
SEQUENCE 699 AA; 80064 MW; 78A6E490AE48E508 CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VADKVVVTTK HNDDEQYVWE SQAGGSFTVT RDTSGETLGR GTKMVLYLKE
DQLEYLEERR LKDLVKKHSE FISYPISLWI EKTIEKEISD DEEEEEKKDE EGKVEEVDEE
KEKEEKKKKK IKEVSHEWDL VNKQKPIWMR KPEEINKEEY AAFYKSLSND WEEHLAVKHF
SVEGQLEFKA ILFVPKRAPF DLFDTKKKPN NIKLYVRRVF IMDNCEDIIP EYLGFVKGIV
DSEDLPLNIS RETLQQNKIL KVIRKNLVKK CLELFFEIAE NKEDYNKFYE AFSKNLKLGI
HEDSQNRTKI AELLRYHSTK SGDELTSLKD YVTRMKEGQN DIFYITGESK KAVENSPFLE
KLKKKGIEVL YMVDAIDEYA IGQLKEFEGK KLVSATKEGL KLDETEDEKK KKEELKEKFE
GLCKVIKDVL GDKVEKVIVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDSSMAGYMS
SKKTMEINPE NSIMDELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLD EPNTFGSRIH
RMLKLGLSID DDDAVEADAE MPPLEDDADA EGSKMEEVD


Related products :

Catalog number Product name Quantity
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 96T
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.2 mg
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
E0693h ELISA kit 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive pro 96T
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.1 mg
E0693m ELISA kit Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T


 

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