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60 kDa heat shock protein, mitochondrial (EC 3.6.4.9) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (HSP-65) (Heat shock protein 60) (HSP-60) (Hsp60) (Mitochondrial matrix protein P1)

 CH60_RAT                Reviewed;         573 AA.
P63039; P19226; P19227; P97602;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 1.
22-NOV-2017, entry version 127.
RecName: Full=60 kDa heat shock protein, mitochondrial;
EC=3.6.4.9;
AltName: Full=60 kDa chaperonin;
AltName: Full=Chaperonin 60;
Short=CPN60;
AltName: Full=HSP-65;
AltName: Full=Heat shock protein 60;
Short=HSP-60;
Short=Hsp60;
AltName: Full=Mitochondrial matrix protein P1;
Flags: Precursor;
Name=Hspd1; Synonyms=Hsp60;
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].
STRAIN=Wistar; TISSUE=Liver;
PubMed=1979858; DOI=10.1093/nar/18.23.7162;
Peralta D., Hartman D.J., McIntosh A.M., Hoogenraad N.J., Hoej P.B.;
"cDNA and deduced amino acid sequence of rat liver prehsp60
(chaperonin-60).";
Nucleic Acids Res. 18:7162-7162(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley, and Wistar;
Ryan M.T., Herd S.M., Sberna G., Samuel M.M., Hoogenraad N.J.,
Hoej P.B.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-573.
TISSUE=Kidney;
PubMed=1976241; DOI=10.1093/nar/18.17.5309;
Venner T.J., Gupta R.S.;
"Nucleotide sequence of rat hsp60 (chaperonin, GroEL homolog) cDNA.";
Nucleic Acids Res. 18:5309-5309(1990).
[5]
PROTEIN SEQUENCE OF 38-58; 61-72; 143-157; 222-233; 237-309; 345-352;
371-387; 397-405; 421-446; 463-469 AND 482-493, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, 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: Chaperonin implicated in mitochondrial protein import
and macromolecular assembly. Together with Hsp10, facilitates the
correct folding of imported proteins. May also prevent misfolding
and promote the refolding and proper assembly of unfolded
polypeptides generated under stress conditions in the
mitochondrial matrix. The functional units of these chaperonins
consist of heptameric rings of the large subunit Hsp60, which
function as a back-to-back double ring. In a cyclic reaction,
Hsp60 ring complexes bind one unfolded substrate protein per ring,
followed by the binding of ATP and association with 2 heptameric
rings of the co-chaperonin Hsp10. This leads to sequestration of
the substrate protein in the inner cavity of Hsp60 where, for a
certain period of time, it can fold undisturbed by other cell
components. Synchronous hydrolysis of ATP in all Hsp60 subunits
results in the dissociation of the chaperonin rings and the
release of ADP and the folded substrate protein.
{ECO:0000250|UniProtKB:P10809}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:P10809}.
-!- SUBUNIT: Homoheptamer arranged in a ring structure. The functional
units of these chaperonins consist of heptameric rings of the
large subunit Hsp60, which function as a back-to-back double ring.
Interacts with 2 heptameric Hsp10 rings to form the symmetrical
football complex (By similarity). Interacts with HRAS (By
similarity). Interacts with ATAD3A. Interacts with ETFBKMT and
METTL21B (By similarity). {ECO:0000250|UniProtKB:P10809,
ECO:0000250|UniProtKB:P63038}.
-!- INTERACTION:
Q63690:Bax; NbExp=2; IntAct=EBI-432091, EBI-822405;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:P10809}.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000305}.
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EMBL; X54793; CAA38564.1; -; mRNA.
EMBL; U68562; AAC53362.1; -; Genomic_DNA.
EMBL; BC086507; AAH86507.1; -; mRNA.
EMBL; X53585; CAA37654.1; -; mRNA.
PIR; S13089; HHRT60.
RefSeq; NP_071565.2; NM_022229.2.
RefSeq; XP_006244994.1; XM_006244932.2.
UniGene; Rn.102058; -.
UniGene; Rn.129767; -.
ProteinModelPortal; P63039; -.
SMR; P63039; -.
BioGrid; 248912; 5.
CORUM; P63039; -.
IntAct; P63039; 7.
MINT; MINT-1860257; -.
STRING; 10116.ENSRNOP00000063666; -.
iPTMnet; P63039; -.
PhosphoSitePlus; P63039; -.
World-2DPAGE; 0004:P63039; -.
PaxDb; P63039; -.
PRIDE; P63039; -.
Ensembl; ENSRNOT00000066589; ENSRNOP00000063666; ENSRNOG00000014525.
GeneID; 63868; -.
KEGG; rno:63868; -.
UCSC; RGD:621314; rat.
CTD; 3329; -.
RGD; 621314; Hspd1.
eggNOG; KOG0356; Eukaryota.
eggNOG; COG0459; LUCA.
GeneTree; ENSGT00390000005727; -.
HOGENOM; HOG000076290; -.
HOVERGEN; HBG001982; -.
InParanoid; P63039; -.
KO; K04077; -.
OMA; TDTDKME; -.
OrthoDB; EOG091G04JM; -.
PhylomeDB; P63039; -.
TreeFam; TF300475; -.
PRO; PR:P63039; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000014525; -.
Genevisible; P63039; RN.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
GO; GO:0030135; C:coated vesicle; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005769; C:early endosome; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
GO; GO:0046696; C:lipopolysaccharide receptor complex; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043209; C:myelin sheath; ISO:RGD.
GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0042588; C:zymogen granule; IDA:RGD.
GO; GO:0034186; F:apolipoprotein A-I binding; ISO:RGD.
GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051087; F:chaperone binding; ISO:RGD.
GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:RGD.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0043559; F:insulin binding; IPI:RGD.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
GO; GO:0051787; F:misfolded protein binding; IPI:RGD.
GO; GO:0002039; F:p53 binding; ISO:RGD.
GO; GO:0002020; F:protease binding; IPI:RGD.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0006458; P:'de novo' protein folding; IC:RGD.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:RGD.
GO; GO:0042113; P:B cell activation; ISO:RGD.
GO; GO:0002368; P:B cell cytokine production; ISO:RGD.
GO; GO:0042100; P:B cell proliferation; ISO:RGD.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:RGD.
GO; GO:0002236; P:detection of misfolded protein; IDA:RGD.
GO; GO:0051702; P:interaction with symbiont; ISO:RGD.
GO; GO:0048291; P:isotype switching to IgG isotypes; ISO:RGD.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow; IMP:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0050729; P:positive regulation of inflammatory response; IDA:RGD.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:RGD.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:RGD.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:RGD.
GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD.
GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; ISO:RGD.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:RGD.
GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
GO; GO:0042026; P:protein refolding; ISO:RGD.
GO; GO:0050821; P:protein stabilization; ISO:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0033198; P:response to ATP; IEP:RGD.
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:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0006986; P:response to unfolded protein; ISO:RGD.
GO; GO:0042110; P:T cell activation; ISO:RGD.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 2.
Gene3D; 3.50.7.10; -; 1.
HAMAP; MF_00600; CH60; 1.
InterPro; IPR018370; Chaperonin_Cpn60_CS.
InterPro; IPR001844; Chaprnin_Cpn60.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR037290; Cpn60/TCP-1_sf.
InterPro; IPR027409; GroEL-like_apical_dom_sf.
InterPro; IPR027413; GROEL-like_equatorial_sf.
PANTHER; PTHR11353; PTHR11353; 1.
Pfam; PF00118; Cpn60_TCP1; 1.
PRINTS; PR00298; CHAPERONIN60.
SUPFAM; SSF48592; SSF48592; 2.
SUPFAM; SSF52029; SSF52029; 1.
SUPFAM; SSF54849; SSF54849; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Chaperone; Complete proteome;
Direct protein sequencing; Hydrolase; Isopeptide bond; Mitochondrion;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Transit peptide; Ubl conjugation.
TRANSIT 1 26 Mitochondrion. {ECO:0000250}.
CHAIN 27 573 60 kDa heat shock protein, mitochondrial.
/FTId=PRO_0000005029.
NP_BIND 111 115 ATP. {ECO:0000250|UniProtKB:P10809}.
BINDING 75 75 ATP. {ECO:0000250|UniProtKB:P10809}.
BINDING 440 440 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:P10809}.
BINDING 520 520 ATP. {ECO:0000250|UniProtKB:P10809}.
MOD_RES 31 31 N6-succinyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 75 75 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 82 82 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 82 82 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 87 87 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 91 91 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 125 125 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 125 125 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 130 130 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 133 133 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 133 133 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 133 133 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 156 156 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 191 191 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 191 191 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 202 202 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 202 202 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 205 205 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 205 205 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 218 218 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 218 218 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 236 236 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 236 236 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 249 249 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 250 250 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 250 250 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 269 269 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 292 292 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 301 301 N6-succinyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 314 314 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 352 352 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 352 352 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 359 359 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 389 389 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 396 396 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 396 396 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 455 455 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 455 455 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 469 469 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10809}.
MOD_RES 481 481 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 481 481 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63038}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000250|UniProtKB:P10809}.
CROSSLNK 551 551 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P10809}.
CONFLICT 121 121 R -> P (in Ref. 2; AAC53362).
{ECO:0000305}.
CONFLICT 537 537 S -> P (in Ref. 1; CAA38564).
{ECO:0000305}.
SEQUENCE 573 AA; 60955 MW; 0014B58B77D0127B CRC64;
MLRLPTVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK
DIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ
DAYVLLSEKK ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV TKDDAMLLKG
KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR
VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLKPANED QKIGIEIIKR ALKIPAMTIA
KNAGVEGSLI VEKILQSSSE VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT
TAEAVVTEIP KEEKDPGMGA MGGMGGGMGG GMF


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E0822c ELISA 60 kDa chaperonin,60 kDa heat shock protein, mitochondrial,Chaperonin 60,Chicken,CPN60,Gallus gallus,Heat shock protein 60,Hsp60,HSP60,HSP-60,HSPD1,RCJMB04_7g5 96T
U0822c CLIA 60 kDa chaperonin,60 kDa heat shock protein, mitochondrial,Chaperonin 60,Chicken,CPN60,Gallus gallus,Heat shock protein 60,Hsp60,HSP60,HSP-60,HSPD1,RCJMB04_7g5 96T
U0822c CLIA 60 kDa chaperonin,60 kDa heat shock protein, mitochondrial,Canis familiaris,Canis lupus familiaris,Chaperonin 60,CPN60,Dog,Heat shock protein 60,Hsp60,HSP60,HSP-60,HSPD1 96T
E0822c ELISA kit 60 kDa chaperonin,60 kDa heat shock protein, mitochondrial,Canis familiaris,Canis lupus familiaris,Chaperonin 60,CPN60,Dog,Heat shock protein 60,Hsp60,HSP60,HSP-60,HSPD1 96T
E0822c ELISA 60 kDa chaperonin,60 kDa heat shock protein, mitochondrial,Canis familiaris,Canis lupus familiaris,Chaperonin 60,CPN60,Dog,Heat shock protein 60,Hsp60,HSP60,HSP-60,HSPD1 96T
10-002-38019 GroEL (1-548aa) - Hsp60; 60 kDa chaperonin; CPN60; Heat shock protein 60; HSP-60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HuCHA60 N_A 1 mg
E1501r ELISA 10 kDa chaperonin,10 kDa heat shock protein, mitochondrial,Chaperonin 10,CPN10,Hsp10,Hspe1,Rat,Rattus norvegicus 96T
E1501m ELISA kit 10 kDa chaperonin,10 kDa heat shock protein, mitochondrial,Chaperonin 10,CPN10,Hsp10,Hspe1,Mouse,Mus musculus 96T
E1501r ELISA kit 10 kDa chaperonin,10 kDa heat shock protein, mitochondrial,Chaperonin 10,CPN10,Hsp10,Hspe1,Rat,Rattus norvegicus 96T
E1501b ELISA 10 kDa chaperonin,10 kDa heat shock protein, mitochondrial,Bos taurus,Bovine,Chaperonin 10,CPN10,Hsp10,HSPE1 96T
E1501b ELISA kit 10 kDa chaperonin,10 kDa heat shock protein, mitochondrial,Bos taurus,Bovine,Chaperonin 10,CPN10,Hsp10,HSPE1 96T
U1501b CLIA 10 kDa chaperonin,10 kDa heat shock protein, mitochondrial,Bos taurus,Bovine,Chaperonin 10,CPN10,Hsp10,HSPE1 96T


 

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