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This locus encodes a heat shock protein. Additionally we are shipping Heat Shock Protein, alpha-Crystallin-Related, B6 Antibodies (95) and Heat Shock Protein, alpha-Crystallin-Related, B6 Kits (26) and many more products for this protein.
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HSPB6 is expressed during development.
Structural basis for the interaction of a human HSPB6 protein with the 14-3-3 (show YWHAQ Proteins) universal signaling regulator has been reported.
Data suggest that HSPB6 forms hetero-oligomers with HSPB1 under the following rules: (1) highly conserved motif RLFDQXFG is necessary for subunit exchange among oligomers, (2) a site about 20 residues downstream of this motif determines size of resultant hetero-oligomers, and (3) a region in the N-terminal domain that is unique to HSPB6 dictates preferential formation of heterodimers. (HSP = heat shock protein)
findings strongly suggest that phosphorylated HSP20 inhibits TGF-alpha (show TGFA Proteins)-induced HCC (show FAM126A Proteins) cell migration and invasion via suppression of the JNK (show MAPK8 Proteins) signaling pathway
multiple sclerosis lesions revealed exclusive induction of HSPB6 in astrocytes, as confirmed by co-localization of HSPB6 with GFAP (show GFAP Proteins).
N-terminal mutations increase stability of large HspB1 (show HSPB1 Proteins) homooligomers, prevent their phosphorylation-dependent dissociation, modulate their interaction with HspB6 and decrease their chaperoning capacity, preventing normal functioning of HspB1 (show HSPB1 Proteins).
Findings strongly suggest that HSP20 directly associates with Bax (show BAX Proteins) and stimulates caspase (show CASP3 Proteins) cascade in human hepatocellular carcinoma cells.
Data suggest that heat shock protein 20 (HSP20) may have value as a prognostic tumor marker and its overexpression might be a novel strategy for colorectal cancer (CRC (show CALR Proteins)) therapy.
peptides in heat-shock protein Hsp20 (show HSP20 Proteins) (G71HFSVLLDVKHFSPEEIAVK91) and Hsp27 (show HSPB1 Proteins) (D93RWRVSLDVNHFAPDELTVK113) with sequence homology to alpha-crystallin also have robust chaperone and anti-apoptotic activities.
These findings strongly suggest that HSP20 might decrease the IKK-alpha (show CHUK Proteins) protein level and that it down-regulates the TNF-alpha (show TNF Proteins)-stimulated intracellular signaling in HCC (show FAM126A Proteins), thus resulting in the suppression of HCC (show FAM126A Proteins) progression.
HSP20 may play a protective role against the progression of ovarian cancer.
HSP20 is associated with both actin and alpha-actinin (show ACTN1 Proteins); activation of cyclic nucleotide-dependent signaling pathways leads to increases in the phosphorylation of HSP20 and a decrease in the association of HSP20 with alpha-actinin (show ACTN1 Proteins).
Increased expression of Hsp20 in neuroblastoma (show ARHGEF16 Proteins) cells protected against ischemia-reperfusion injury.
potential protein targets for the loss of PostC may include F(1)-ATPase gamma, Echs1 (show ECHS1 Proteins) and Hsp20 that could regulate cellular ATP consumption/production and defense response to ischaemic stress
the activity of type 1 protein phosphatase (PP1 (show PPP1CC Proteins)), a known regulator of PLN (show PLN Proteins) signaling, was significantly reduced by Hsp20 overexpression, suggesting that the Hsp20 stimulatory effects are partially mediated through the PP1 (show PPP1CC Proteins)-PLN (show PLN Proteins) axis.
identification and characterization of a cardiac isoform of p20 associated with beta-adrenergic signaling in adult cardiomyocytes.
Recombinant mouse Hsp20 translocates to and interacts with actin cytoskeleton in response to isoproterenol stimulation and prevents ss-agonist-induced apoptosis in adult rat cardiomyocytes.
miR (show MLXIP Proteins)-320 is involved in the regulation of I/R-induced cardiac injury and dysfunction via antithetical regulation of Hsp20
Hsp20 expression prevents endotoxin-induced myocardial dysfunction and apoptosis via inhibition of NF-kappaB (show NFKB1 Proteins) activation
Blockade of Hsp20 phosphorylation exacerbates cardiac ischemia/reperfusion injury by suppressed autophagy and increased cell death.
HSPB6 cDNA encodes a 168 aa protein that contains an alpha-crystallin domain, a polar C-terminal extension and some possible phosphorylation sites. HSPB6 shares 94% identity with a X. tropicalis HSPB6, 65% with turtle, 59% with humans, 49% with zebrafish and only 50% and 43% with X. laevis HSPB1 and HSP30C, respectively.
This locus encodes a heat shock protein. The encoded protein likely plays a role in smooth muscle relaxation.
, small heat shock protein HSPB6
, heat shock protein, alpha-crystallin-related, B6
, heat shock 20 kDa-like protein p20
, heat shock protein beta-6
, heat shock 20-kDa protein
, cardiac heat shock protein p20
, cardiac p20