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Human HSPD1 Protein expressed in Escherichia coli (E. coli) - ABIN1686673
Bukau, Horwich: The Hsp70 and Hsp60 chaperone machines. in Cell 1998
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Bacteria HSPD1 Protein expressed in Escherichia coli (E. coli) - ABIN1686691
Koll, Guiard, Rassow, Ostermann, Horwich, Neupert, Hartl: Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. in Cell 1992
Show all 5 Pubmed References
Human HSPD1 Protein expressed in Escherichia coli (E. coli) - ABIN2004223
Rasmussen, Ji, Eddes, Moritz, Reid, Simpson, Dorow: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. in Electrophoresis 1997
Show all 5 Pubmed References
Expression of HSP60A is post-transcriptionally regulated in a highly dynamic pattern during embryogenesis, even under heat-shock conditions. In contrast, in very stressful situations, its expression is upregulated transcriptionally over the entire embryo.
Heat-shock protein 60 is required for blastema formation and maintenance during regeneration.
HSP60 regulation of SOX9 (zeige SOX9 Proteine) ubiquitination mitigates the development of knee osteoarthritis.
These findings shed some light on how a tumor cell may avert apoptosis using Hsp60 and point to the anti-cancer potential of drugs, such as CubipyOXA, which interfere with Hsp60/pC3 (zeige PCSK1 Proteine) complex formation, and thus allow the apoptotic cascade to proceed.
The associations of diabetes, combined with the polymorphisms in the genes of fat mass and obesity-associated (zeige FTO Proteine) gene (FTO (zeige FTO Proteine)), interleukin 6 (IL-6 (zeige IL6 Proteine)), and heat shock protein 60 (HSPD1), with breast cancer risk and survival in a Chinese Han population, was evaluated.
27-Hydroxycholesterol upregulates the production of HSP60 in monocytic cells.
data indicate that HSP65 suppresses cholesterol efflux and increases cellular cholesterol content through an Lck (zeige LCK Proteine)-mediated pathway in T cells
Doxorubicin treatment of lung mucoepidermoid cells results in Hsp60 post-translational modifications leading to the Hsp60/p53 (zeige TP53 Proteine) complex dissociation and instauration of replicative senescence.
Phosphorylation and subsequent transient degradation of mitochondrial Hsp60 during early hours of rotavirus-SA11 infection resulted in inhibition of premature import of nonstructural protein 4 into mitochondria, thereby delaying early apoptosis.
Data show that the interaction between cell cycle and apoptosis regulator 2 (CCAR2) and heat shock protein 60 (Hsp60) increases in the presence of rotenone.
NIP (zeige GIPC1 Proteine)-SNAP-1 (zeige NIPSNAP3B Proteine) and -2 localized in the mitochondrial inner membrane space, whereas HSP60 localized in the matrix. Expression levels of NIP (zeige GIPC1 Proteine)-SNAP-1 (zeige NIPSNAP3B Proteine) and -2 in cells were decreased by knockdown of HSP60, but not HSP10 (zeige HSPE1 Proteine). The findings indicate that HSP60 promotes folding and maintains the stability of NIP (zeige GIPC1 Proteine)-SNAP-1 (zeige NIPSNAP3B Proteine) and -2.
In this instance, the ATP5B (zeige ATP5B Proteine)/CALR (zeige CALR Proteine)/HSP90B1 (zeige HSP90B1 Proteine)/HSPB1 (zeige HSPB1 Proteine)/HSPD1-signaling network was revealed as the predominant target which was associated with the majority of the observed protein-protein interactions. As a result, the identified targets may be useful in explaining the anticancer mechanisms of ursolic acid and as potential targets for colorectal cancer therapy.
Wild type HSP60 displayed a heptameric single-ring structure in the absence of ATP. In contrast, HSP60 formed mainly a "football-type" complex with HSP10 (zeige HSPE1 Proteine) in the presence of ATP and mediated the refolding of denatured substrate protein.
These results indicate that different tissues had different sensitivities to transport stress, possibly resulting in varying levels of cytoprotection by Hsp60 in the different tissues.
This paper reports the localization of both GRP78 (zeige HSPA5 Proteine) and HSP60 on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 in the sperm midpiece.
Overexpressing hsp60 in cultured myoblasts induced only the expression of PGC1 1alpha, suggesting a correlation between Hsp60 overexpression and PGC1 1 alpha activation.
neonatal heart failure through HSP60 induction likely involves developmental defects and excessive apoptosis
Heat shock protein 60 stimulates the migration of vascular smooth muscle cells via Toll-like receptor 4 (zeige TLR4 Proteine) and ERK MAPK (zeige MAPK1 Proteine) activation
TLR4 (zeige TLR4 Proteine) mediates HSP60-associated apoptosis and that HSP60 has an important role in cardiac myocyte injury, both apoptotic and necrotic.
a direct toxic effect of heat shock protein 60 towards neurons and oligodendrocytes in the CNS involving Toll (zeige TLR4 Proteine)-like receptor4 and MyD88 (zeige MYD88 Proteine) pathways
Dietary wolfberry elevated the xanthophyll concentrations and enhanced expression of BCO2 and heat shock protein 60, activated AMPKalpha2 (zeige PRKAA2 Proteine), potentiated mitophagy and mitochondrial biogenesis and enhanced lipid oxidation and secretion in the liver of mice.
It is concluded that nasal administration of HSP60 can inhibit atherosclerotic formation through immune tolerance which is established by Tregs depending on the induction of anti-inflammatory cytokine TGF-beta (zeige TGFB1 Proteine).
MnSOD (zeige SOD2 Proteine) is a substrate of the Hsp60 folding machinery.
In type 2 diabetes, there is hypothalamic insulin (zeige INS Proteine) resistance and mitochondrial dysfunction due to downregulation of the mitochondrial chaperone HSP60. HSP60 reduction was due to a lack of proper leptin (zeige LEP Proteine) signaling and was restored by leptin (zeige LEP Proteine) treatment.
This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13.
60-kDa heat shock protein, mitochondrial
, Hsp 60
, heat shock protein 60
, heat shock protein 60 kDa
, mitochondrial matrix protein P1
, 60 kDa heat shock protein, mitochondrial
, heat shock 60kDa protein 1 (chaperonin)
, 60 kDa heat shock protein, mitochondrial-like
, chaperonin GroEL
, mitochondrial chaperonin
, no blastema
, 60 kDa chaperonin
, P60 lymphocyte protein
, chaperonin 60
, heat shock protein 65
, short heat shock protein 60 Hsp60s1
, heat shock 60 kDa protein 1
, mitochondrial heat shock 60 kDa protein 1
, heat shock protein, 60 kDa
, heat shock 60kD protein 1 (chaperonin)
, heat shock 60kDa protein 1
, heat shock protein 60 (liver)