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Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86)

 HS90A_RAT               Reviewed;         733 AA.
P82995; Q91XW0;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 143.
RecName: Full=Heat shock protein HSP 90-alpha;
AltName: Full=Heat shock 86 kDa;
Short=HSP 86;
Short=HSP86;
Name=Hsp90aa1; Synonyms=Hsp86, Hspca;
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 [GENOMIC DNA].
TISSUE=Brain;
Li C.W., Chang M.T., Lai Y., Chang W.M., Lai Y.K.;
"Cloning of rat 86-kDa heat shock protein gene and promoter.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Lai Y.R., Chang M.D., Chang W.M., Su C.Y., Lai Y.K.;
"Cloning of full length cDNA of rat 86-kDa heat shock protein gene.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart, and 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).
[4]
PROTEIN SEQUENCE OF 2-13.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=11732320; DOI=10.1007/BF01288360;
Langer T., Fasold H.;
"Isolation and quantification of the heat shock protein 90 alpha and
beta isoforms from rat liver.";
Protoplasma 218:54-56(2001).
[5]
PROTEIN SEQUENCE OF 154-173; 329-339 AND 347-356, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[6]
INTERACTION WITH SGTA.
PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
Liou S.T., Wang C.;
"Small glutamine-rich tetratricopeptide repeat-containing protein is
composed of three structural units with distinct functions.";
Arch. Biochem. Biophys. 435:253-263(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252; SER-263
AND SER-454, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Molecular chaperone that promotes the maturation,
structural maintenance and proper regulation of specific target
proteins involved for instance in cell cycle control and signal
transduction. Undergoes a functional cycle that is linked to its
ATPase activity which is essential for its chaperone activity.
This cycle probably induces conformational changes in the client
proteins, thereby causing their activation. Interacts dynamically
with various co-chaperones that modulate its substrate
recognition, ATPase cycle and chaperone function. Engages with a
range of client protein classes via its interaction with various
co-chaperone proteins or complexes, that act as adapters,
simultaneously able to interact with the specific client and the
central chaperone itself. Recruitment of ATP and co-chaperone
followed by client protein forms a functional chaperone. After the
completion of the chaperoning process, properly folded client
protein and co-chaperone leave HSP90 in an ADP-bound partially
open conformation and finally, ADP is released from HSP90 which
acquires an open conformation for the next cycle. Apart from its
chaperone activity, it also plays a role in the regulation of the
transcription machinery. HSP90 and its co-chaperones modulate
transcription at least at three different levels. In the first
place, they alter the steady-state levels of certain transcription
factors in response to various physiological cues. Second, they
modulate the activity of certain epigenetic modifiers, such as
histone deacetylases or DNA methyl transferases, and thereby
respond to the change in the environment. Third, they participate
in the eviction of histones from the promoter region of certain
genes and thereby turn on gene expression. Binds bacterial
lipopolysaccharide (LPS) and mediates LPS-induced inflammatory
response, including TNF secretion by monocytes. Antagonizes STUB1-
mediated inhibition of TGF-beta signaling via inhibition of STUB1-
mediated SMAD3 ubiquitination and degradation.
{ECO:0000250|UniProtKB:P07900}.
-!- ACTIVITY REGULATION: In the resting state, through the
dimerization of its C-terminal domain, HSP90 forms a homodimer
which is defined as the open conformation. Upon ATP-binding, the
N-terminal domain undergoes significant conformational changes and
comes in contact to form an active closed conformation. After
HSP90 finishes its chaperoning tasks of assisting the proper
folding, stabilization and activation of client proteins under the
active state, ATP molecule is hydrolyzed to ADP which then
dissociates from HSP90 and directs the protein back to the resting
state. Co-chaperone TSC1 promotes ATP binding and inhibits
HSP90AA1 ATPase activity. Binding to phosphorylated AHSA1 promotes
HSP90AA1 ATPase activity. Inhibited by Ganetespib (STA-9090) and
SNX-2112. {ECO:0000250|UniProtKB:P07900}.
-!- SUBUNIT: Homodimer (By similarity). Identified in NR3C1/GCR
steroid receptor-chaperone complexes formed at least by NR3C1,
HSP90AA1 and a variety of proteins containing TPR repeats such as
FKBP4, FKBP5, PPID, PPP5C or STIP1 (By similarity). Forms a
complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to
recruit TCS2 to the complex (By similarity). The closed form
interacts (via the middle domain and TPR repeat-binding motif)
with co-chaperone TSC1 (via C-terminus) (By similarity). Interacts
with TOM34 (By similarity). Interacts with TERT; the interaction,
together with PTGES3, is required for correct assembly and
stabilization of the TERT holoenzyme complex (By similarity).
Interacts with CHORDC1 and DNAJC7 (By similarity). Interacts with
STUB1 and UBE2N; may couple the chaperone and ubiquitination
systems (By similarity). Interacts (via TPR repeat-binding motif)
with PPP5C (via TPR repeats); the interaction is direct and
activates PPP5C phosphatase activity (By similarity). Following
LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (By
similarity). Interacts with KSR1 (By similarity). Interacts with
co-chaperone CDC37 (via C-terminus); the interaction inhibits
HSP90AA1 ATPase activity (By similarity). May interact with NWD1
(By similarity). Interacts with FNIP1 and FNIP2; the interaction
inhibits HSP90AA1 ATPase activity (By similarity). Interacts with
co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the interaction
activates HSP90AA1 ATPase activity and results in the dissociation
of TSC1 from HSP90AA1 (By similarity). Interacts with FLCN in the
presence of FNIP1 (By similarity). Interacts with HSP70, STIP1 and
PTGES3 (By similarity). Interacts with SGTA (via TPR repeats)
(PubMed:15708368). Interacts with SMYD3; this interaction enhances
SMYD3 histone-lysine N-methyltransferase (By similarity).
Interacts with TTC1 (via TPR repeats) (By similarity). Interacts
with HSF1 in an ATP-dependent manner (By similarity). Interacts
with MET; the interaction suppresses MET kinase activity (By
similarity). Interacts with ERBB2 in an ATP-dependent manner; the
interaction suppresses ERBB2 kinase activity (By similarity).
Interacts with HIF1A, KEAP1 and RHOBTB2 (By similarity). Interacts
with HSF1; this interaction is decreased in a IER5-dependent
manner, promoting HSF1 accumulation in the nucleus,
homotrimerization and DNA-binding activities. Interacts with STUB1
and SMAD3 (By similarity). Interacts with HSP90AB1; interaction is
constitutive (By similarity). Interacts with HECTD1 (via N-
terminus) (By similarity). {ECO:0000250|UniProtKB:P07900,
ECO:0000250|UniProtKB:P07901, ECO:0000269|PubMed:15708368}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}.
Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome
{ECO:0000250|UniProtKB:P07900}. Cell membrane
{ECO:0000250|UniProtKB:P07900}.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins like the co-chaperone STUB1.
{ECO:0000250|UniProtKB:P07900}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P07900}.
-!- PTM: S-nitrosylated; negatively regulates the ATPase activity and
the activation of eNOS by HSP90AA1.
{ECO:0000250|UniProtKB:P07900}.
-!- PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by
HECTD1. Ubiquitination promotes translocation into the cytoplasm
away from the membrane and secretory pathways.
{ECO:0000250|UniProtKB:P07901}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; AJ297736; CAC39453.1; -; Genomic_DNA.
EMBL; AJ428213; CAD21648.1; -; mRNA.
EMBL; BC072489; AAH72489.1; -; mRNA.
EMBL; BC085120; AAH85120.1; -; mRNA.
RefSeq; NP_786937.1; NM_175761.2.
RefSeq; XP_008763191.1; XM_008764969.2.
UniGene; Rn.119867; -.
UniGene; Rn.231905; -.
UniGene; Rn.232226; -.
UniGene; Rn.3277; -.
ProteinModelPortal; P82995; -.
SMR; P82995; -.
BioGrid; 256205; 20.
CORUM; P82995; -.
IntAct; P82995; 4.
MINT; P82995; -.
STRING; 10116.ENSRNOP00000009556; -.
CarbonylDB; P82995; -.
iPTMnet; P82995; -.
PaxDb; P82995; -.
PRIDE; P82995; -.
Ensembl; ENSRNOT00000009556; ENSRNOP00000009556; ENSRNOG00000007219.
Ensembl; ENSRNOT00000086310; ENSRNOP00000075715; ENSRNOG00000059714.
GeneID; 103692716; -.
GeneID; 299331; -.
KEGG; rno:103692716; -.
KEGG; rno:299331; -.
UCSC; RGD:631409; rat.
CTD; 3320; -.
RGD; 631409; Hsp90aa1.
eggNOG; KOG0019; Eukaryota.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00940000153658; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P82995; -.
KO; K04079; -.
OMA; VKRHSEF; -.
OrthoDB; EOG091G0270; -.
PhylomeDB; P82995; -.
TreeFam; TF300686; -.
Reactome; R-RNO-1227986; Signaling by ERBB2.
Reactome; R-RNO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-203615; eNOS activation.
Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-RNO-3371511; HSF1 activation.
Reactome; R-RNO-3371568; Attenuation phase.
Reactome; R-RNO-3371571; HSF1-dependent transactivation.
Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-RNO-8854518; AURKA Activation by TPX2.
Reactome; R-RNO-8863795; Downregulation of ERBB2 signaling.
Reactome; R-RNO-8939211; ESR-mediated signaling.
Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
PRO; PR:P82995; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000007219; Expressed in 9 organ(s), highest expression level in testis.
Genevisible; P82995; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0044294; C:dendritic growth cone; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; NAS:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; ISS:AgBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0036126; C:sperm flagellum; IDA:RGD.
GO; GO:0097226; C:sperm mitochondrial sheath; IDA:RGD.
GO; GO:0097524; C:sperm plasma membrane; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0002135; F:CTP binding; IDA:RGD.
GO; GO:0032564; F:dATP binding; IDA:RGD.
GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0044325; F:ion channel binding; IPI:RGD.
GO; GO:0003729; F:mRNA binding; IDA:RGD.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IPI:RGD.
GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IDA:RGD.
GO; GO:0017098; F:sulfonylurea receptor binding; IPI:RGD.
GO; GO:0048156; F:tau protein binding; IPI:RGD.
GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0002134; F:UTP binding; IDA:RGD.
GO; GO:0048675; P:axon extension; IEA:Ensembl.
GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEP:RGD.
GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
GO; GO:0061684; P:chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IMP:RGD.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEP:RGD.
GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:RGD.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0006457; P:protein folding; TAS:RGD.
GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
GO; GO:0061635; P:regulation of protein complex stability; NAS:ParkinsonsUK-UCL.
GO; GO:0046677; P:response to antibiotic; ISS:AgBase.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0009409; P:response to cold; ISS:AgBase.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
GO; GO:0003009; P:skeletal muscle contraction; IEP:RGD.
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;
Acetylation; ATP-binding; Cell membrane; Chaperone; Complete proteome;
Cytoplasm; Direct protein sequencing; Membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; S-nitrosylation;
Stress response; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11732320}.
CHAIN 2 733 Heat shock protein HSP 90-alpha.
/FTId=PRO_0000062915.
REGION 285 733 Interaction with FLCN and FNIP1.
{ECO:0000250|UniProtKB:P07900}.
REGION 285 621 Interaction with FNIP2 and TSC1.
{ECO:0000250|UniProtKB:P07900}.
REGION 683 733 Required for homodimerization.
{ECO:0000250|UniProtKB:P07900}.
REGION 729 733 Essential for interaction with SMYD3,
TSC1 and STIP1/HOP.
{ECO:0000250|UniProtKB:P07900}.
REGION 730 733 Essential for interaction with SGTA and
TTC1. {ECO:0000250|UniProtKB:P07900}.
MOTIF 724 733 TPR repeat-binding.
{ECO:0000250|UniProtKB:P07900}.
BINDING 51 51 ATP. {ECO:0000250}.
BINDING 93 93 ATP. {ECO:0000250}.
BINDING 112 112 ATP. {ECO:0000250}.
BINDING 138 138 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 401 401 ATP. {ECO:0000250}.
MOD_RES 5 5 Phosphothreonine; by PRKDC.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 7 7 Phosphothreonine; by PRKDC.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 58 58 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 84 84 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 314 314 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 444 444 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 459 459 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 490 490 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 493 493 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07901}.
MOD_RES 586 586 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 599 599 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P07900}.
MOD_RES 642 642 Phosphoserine.
{ECO:0000250|UniProtKB:P07900}.
SEQUENCE 733 AA; 84815 MW; DF2C8383A6581D07 CRC64;
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR
YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM
GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE
KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN
NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK
CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD
YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK
TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV
KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTVDDTS AAVTEEMPPL
EGDDDTSRME EVD


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E0863h ELISA kit Heat shock 86 kDa,Heat shock protein HSP 90-alpha,Homo sapiens,HSP 86,HSP86,HSP90A,HSP90AA1,HSPC1,HSPCA,Human,Renal carcinoma antigen NY-REN-38 96T
27-259 HSF2 binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stres 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 1 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 0.05 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
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
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
25-272 The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced 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
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 0.05 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 0.2 mg
E0693m ELISA 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
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
U0693m CLIA 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
20-372-60095 heat shock 70kDa protein 1-like - Mouse monoclonal anti-human HSPA1L antibody; Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1-Hom; HSP70-Hom Monoclonal 0.1 mg


 

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