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78 kDa glucose-regulated protein (GRP-78) (Heat shock 70 kDa protein 5) (Immunoglobulin heavy chain-binding protein) (BiP) (Steroidogenesis-activator polypeptide)

 BIP_RAT                 Reviewed;         654 AA.
P06761;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
20-JUN-2018, entry version 173.
RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000250|UniProtKB:P11021};
EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
AltName: Full=78 kDa glucose-regulated protein {ECO:0000250|UniProtKB:P11021};
Short=GRP-78 {ECO:0000250|UniProtKB:P11021};
AltName: Full=Binding-immunoglobulin protein {ECO:0000250|UniProtKB:P11021};
Short=BiP {ECO:0000250|UniProtKB:P11021};
AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000250|UniProtKB:P11021};
Short=HSP70 family protein 5 {ECO:0000250|UniProtKB:P11021};
AltName: Full=Heat shock protein family A member 5 {ECO:0000250|UniProtKB:P11021};
AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000250|UniProtKB:P11021};
AltName: Full=Steroidogenesis-activator polypeptide {ECO:0000303|PubMed:3563495};
Flags: Precursor;
Name=Hspa5 {ECO:0000312|RGD:2843};
Synonyms=Grp78 {ECO:0000250|UniProtKB:P11021};
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].
PubMed=3087629; DOI=10.1016/0092-8674(86)90746-4;
Munro S., Pelham H.R.B.;
"An Hsp70-like protein in the ER: identity with the 78 kd glucose-
regulated protein and immunoglobulin heavy chain binding protein.";
Cell 46:291-300(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
PubMed=3468506; DOI=10.1073/pnas.84.3.680;
Chang S.C., Wooden S.K., Nakaki T., Kim Y.K., Lin A.Y., Kung L.,
Attenello J.W., Lee A.S.;
"Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its
regulatory sequences and the effect of protein glycosylation on its
expression.";
Proc. Natl. Acad. Sci. U.S.A. 84:680-684(1987).
[4]
PROTEIN SEQUENCE OF 50-60; 165-181; 307-324; 475-492 AND 533-540, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 626-654.
PubMed=3563495; DOI=10.1126/science.3563495;
Pedersen R.C., Brownie A.C.;
"Steroidogenesis-activator polypeptide isolated from a rat Leydig cell
tumor.";
Science 236:188-190(1987).
[6]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[7]
INTERACTION WITH TMEM132A.
STRAIN=Sprague-Dawley;
PubMed=12514190; DOI=10.1074/jbc.M212083200;
Oh-hashi K., Naruse Y., Amaya F., Shimosato G., Tanaka M.;
"Cloning and characterization of a novel GRP78-binding protein in the
rat brain.";
J. Biol. Chem. 278:10531-10537(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; THR-648 AND SER-649,
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: Endoplasmic reticulum chaperone that plays a key role in
protein folding and quality control in the endoplasmic reticulum
lumen (By similarity). Involved in the correct folding of proteins
and degradation of misfolded proteins via its interaction with
DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5
from its substrate (By similarity). Acts as a key repressor of the
ERN1/IRE1-mediated unfolded protein response (UPR). In the
unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the
luminal region of ERN1/IRE1, leading to disrupt the dimerization
of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of
misfolded protein in the endoplasmic reticulum causes release of
HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent
activation of ERN1/IRE1 (By similarity).
{ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021,
ECO:0000250|UniProtKB:P20029}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:G3I8R9}.
-!- ENZYME REGULATION: The chaperone activity is regulated by ATP-
induced allosteric coupling of the nucleotide-binding (NBD) and
substrate-binding (SBD) domains (By similarity). In the ADP-bound
and nucleotide-free (apo) states, the two domains have little
interaction (By similarity). In contrast, in the ATP-bound state
the two domains are tightly coupled, which results in drastically
accelerated kinetics in both binding and release of polypeptide
substrates (By similarity). J domain-containing co-chaperones
(DNAJB9/ERdj4 or DNAJC10/ERdj5) stimulate the ATPase activity and
are required for efficient substrate recognition by HSPA5/BiP.
Homooligomerization inactivates participating HSPA5/BiP protomers
and probably act as reservoirs to store HSPA5/BiP molecules when
they are not needed by the cell (By similarity).
{ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021}.
-!- SUBUNIT: Monomer and homooligomer; homooligomerization via the
interdomain linker inactivates the chaperone activity and acts as
a storage of HSPA5/BiP molecules (By similarity). Interacts with
DNAJC1 (via J domain) (By similarity). Component of an EIF2
complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1,
EIF2S2, HSP90B1 and HSPA5 (By similarity). Part of a large
chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5,
HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small
amounts of ERP29, but not, or at very low levels, CALR nor CANX
(PubMed:12475965). Interacts with TMEM132A and TRIM21
(PubMed:12514190). May form a complex with ERLEC1, OS9, SEL1L and
SYVN1 (By similarity). Interacts with DNAJC10 (By similarity).
Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to
ERN1/IRE1 (By similarity). Interacts with ERN1/IRE1; interaction
takes place following interaction with DNAJB9/ERdj4 and leads to
inactivate ERN1/IRE1 (By similarity). Interacts with MX1 (By
similarity). Interacts with METTL23 (By similarity). Interacts
with CEMIP; the interaction induces calcium leakage from the
endoplasmic reticulum and cell migration (By similarity).
Interacts with PCSK4 form; the interaction takes place in the
endoplasmic reticulum (By similarity). Interacts with CIPC (By
similarity). Interacts with CCDC88B (via C-terminus); the
interaction opposes ERN1-mediated JNK activation, protecting
against apoptosis (By similarity). Interacts with INPP5K;
necessary for INPP5K localization at the endoplasmic reticulum (By
similarity). Interacts with MANF; the interaction is direct (By
similarity). Interacts with LOXL2; leading to activate the
ERN1/IRE1-XBP1 pathway of the unfolded protein response (By
similarity). {ECO:0000250|UniProtKB:G3I8R9,
ECO:0000250|UniProtKB:P11021, ECO:0000250|UniProtKB:P20029,
ECO:0000269|PubMed:12475965, ECO:0000269|PubMed:12514190}.
-!- INTERACTION:
Q9R0C9:Sigmar1; NbExp=3; IntAct=EBI-916036, EBI-1557826;
P06882:Tg; NbExp=6; IntAct=EBI-916036, EBI-1549657;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000250|UniProtKB:P11021}.
-!- DOMAIN: The interdomain linker regulates the chaperone activity by
mediating the formation of homooligomers. Homooligomers are formed
by engagement of the interdomain linker of one HSPA5/BiP molecule
as a typical substrate of an adjacent HSPA5/BiP molecule.
HSPA5/BiP oligomerization inactivates participating HSPA5/BiP
protomers. HSPA5/BiP oligomers probably act as reservoirs to store
HSPA5/BiP molecules when they are not needed by the cell. When the
levels of unfolded proteins rise, cells can rapidly break up these
oligomers to make active monomers. {ECO:0000250|UniProtKB:G3I8R9}.
-!- PTM: In unstressed cells, AMPylation at Thr-518 by FICD
inactivates the chaperome activity: AMPylated form is locked in a
relatively inert state and only weakly stimulated by J domain-
containing proteins. In response to endoplasmic reticulum stress,
de-AMPylation by the same protein, FICD, restores the chaperone
activity. {ECO:0000250|UniProtKB:G3I8R9}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; M14050; AAA40817.1; -; mRNA.
EMBL; BC062017; AAH62017.1; -; mRNA.
EMBL; M14866; AAA41277.1; -; Genomic_DNA.
PIR; A23948; HHRTGB.
RefSeq; NP_037215.1; NM_013083.2.
UniGene; Rn.11088; -.
ProteinModelPortal; P06761; -.
SMR; P06761; -.
BioGrid; 247646; 7.
CORUM; P06761; -.
IntAct; P06761; 18.
MINT; P06761; -.
STRING; 10116.ENSRNOP00000025064; -.
CarbonylDB; P06761; -.
iPTMnet; P06761; -.
PhosphoSitePlus; P06761; -.
SwissPalm; P06761; -.
PaxDb; P06761; -.
PRIDE; P06761; -.
Ensembl; ENSRNOT00000025067; ENSRNOP00000025064; ENSRNOG00000018294.
GeneID; 25617; -.
KEGG; rno:25617; -.
UCSC; RGD:2843; rat.
CTD; 3309; -.
RGD; 2843; Hspa5.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00910000144045; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P06761; -.
KO; K09490; -.
OMA; CVGVMQK; -.
OrthoDB; EOG091G0352; -.
PhylomeDB; P06761; -.
TreeFam; TF105044; -.
Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
PRO; PR:P06761; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000018294; -.
Genevisible; P06761; RN.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0051787; F:misfolded protein binding; IDA:MGI.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0051082; F:unfolded protein binding; IPI:RGD.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0071277; P:cellular response to calcium ion; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071480; P:cellular response to gamma radiation; IEP:RGD.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0071287; P:cellular response to manganese ion; IEP:ParkinsonsUK-UCL.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
GO; GO:0021589; P:cerebellum structural organization; IEA:Ensembl.
GO; GO:0006983; P:ER overload response; IEA:Ensembl.
GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEP:RGD.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
GO; GO:1904313; P:response to methamphetamine hydrochloride; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0097501; P:stress response to metal ion; IEP:RGD.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Hydrolase;
Isopeptide bond; Methylation; Nitration; Nucleotide-binding;
Phosphoprotein; Reference proteome; Signal; Ubl conjugation.
SIGNAL 1 18 {ECO:0000250}.
CHAIN 19 654 Endoplasmic reticulum chaperone BiP.
/FTId=PRO_0000013569.
NP_BIND 36 39 ATP. {ECO:0000250|UniProtKB:P11021}.
NP_BIND 227 229 ATP. {ECO:0000250|UniProtKB:P11021}.
NP_BIND 293 300 ATP. {ECO:0000250|UniProtKB:P11021}.
NP_BIND 364 367 ATP. {ECO:0000250|UniProtKB:P11021}.
REGION 125 280 Nucleotide-binding (NBD).
{ECO:0000250|UniProtKB:P11021}.
REGION 409 419 Interdomain linker.
{ECO:0000250|UniProtKB:G3I8R9}.
REGION 420 500 Substrate-binding (SBD).
{ECO:0000250|UniProtKB:P11021}.
MOTIF 651 654 Prevents secretion from ER.
BINDING 96 96 ATP. {ECO:0000250|UniProtKB:P11021}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 160 160 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 213 213 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 271 271 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 326 326 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 353 353 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 447 447 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 492 492 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 518 518 O-AMP-threonine; alternate.
{ECO:0000250|UniProtKB:G3I8R9}.
MOD_RES 518 518 Phosphothreonine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 585 585 N6,N6,N6-trimethyllysine; by METTL21A; in
vitro. {ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 585 585 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 585 585 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 591 591 N6-methyllysine.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 643 643 Phosphothreonine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 648 648 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CROSSLNK 352 352 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11021}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11021}.
CONFLICT 29 29 T -> M (in Ref. 3; AAA41277).
{ECO:0000305}.
CONFLICT 649 649 S -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 651 651 K -> KK (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 654 AA; 72347 MW; 9D686C6484150108 CRC64;
MKFTVVAAAL LLLCAVRAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR
ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV
EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ
RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG
VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV
LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC
PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG
TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER
MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSPED KETMEKAVEE
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE KDEL


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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
18-785-210205 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
18-785-210207 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
18-785-210206 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
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
18-785-210208 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
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
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


 

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