Heat Shock Protein, alpha-Crystallin-Related, B6 (HSPB6) ELISA Kits

Human Heat Shock Protein, alpha-Crystallin-Related, B6 (HSPB6) Interaktionspartner

1. these findings reveal a new regulatory mechanism of HSPB6 in cell survival through its interaction with BECN1.

2. Structural basis for the interaction of a human HSPB6 protein with the 14-3-3 universal signaling regulator has been reported.

3. 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)

4. findings strongly suggest that phosphorylated HSP20 inhibits TGF-alpha-induced HCC cell migration and invasion via suppression of the JNK signaling pathway

5. multiple sclerosis lesions revealed exclusive induction of HSPB6 in astrocytes, as confirmed by co-localization of HSPB6 with GFAP.

6. N-terminal mutations increase stability of large HspB1 homooligomers, prevent their phosphorylation-dependent dissociation, modulate their interaction with HspB6 and decrease their chaperoning capacity, preventing normal functioning of HspB1.

7. Findings strongly suggest that HSP20 directly associates with Bax and stimulates caspase cascade in human hepatocellular carcinoma cells.

8. 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) therapy.

9. peptides in heat-shock protein Hsp20 (G71HFSVLLDVKHFSPEEIAVK91) and Hsp27 (D93RWRVSLDVNHFAPDELTVK113) with sequence homology to alpha-crystallin also have robust chaperone and anti-apoptotic activities.

10. These findings strongly suggest that HSP20 might decrease the IKK-alpha protein level and that it down-regulates the TNF-alpha-stimulated intracellular signaling in HCC, thus resulting in the suppression of HCC progression.

11. HSP20 may play a protective role against the progression of ovarian cancer.

12. HSP20 directly associates with PI3K subunits and suppresses its activity in hepatocellular carcinoma, resulting in the inhibition of the AKT pathway, and subsequently decreasing the growth of hepatocellular carcinoma.

13. 14-3-3zeta and possibly other 14-3-3 isoforms may have additional functional roles conducted by the monomeric state

14. the cytosolic protein AKAP-Lbc (AKAP13) as the anchoring protein responsible for directing PKA phosphorylation of Hsp20 on Ser(16)

15. Hsp20 serves as a novel cardiokine in regulating myocardial angiogenesis through activation of the VEGFR signaling cascade.

16. cofilins 1 and 2 only weakly interact with 14-3-3 and therefore cannot directly compete with phosphorylated small heat shock protein HspB6 for its binding to 14-3-3

17. Properties of the monomeric form of 14-3-3zeta protein and its interaction with tau and HspB6. This interaction requires phosphorylation of tau protein and HspB6.

18. A potential molecular mechanism by which Hsp20 acetylation can affect myometrial activity by liberating cofilin

19. Overexpression of HSPB1, as well as HSPB6, HSPB7 and HSPB8 independently protect against tachycardia remodeling by attenuation of the RhoA GTPase pathway at different levels.

20. Nevertheless, in solution, both alpha-crystallin domain proteins form stable dimers via the symmetric antiparallel interaction of beta7 strands.

Mouse (Murine) Heat Shock Protein, alpha-Crystallin-Related, B6 (HSPB6) Interaktionspartner

1. Our study was designed to assess the efficacy of small heat shock proteins B1 (Hsp27) and B6 (Hsp20) as an adjuvant accompanied by HPV16 E7 and hPP10-E7 antigens in tumor mouse model. A major key for successful DNA and protein transfer into cells is the development of delivery systems with high efficiency and low cytotoxicity.

2. Increased expression of Hsp20 in neuroblastoma cells protected against ischemia-reperfusion injury.

3. potential protein targets for the loss of PostC may include F(1)-ATPase gamma, Echs1 and Hsp20 that could regulate cellular ATP consumption/production and defense response to ischaemic stress

4. the activity of type 1 protein phosphatase (PP1), a known regulator of PLN signaling, was significantly reduced by Hsp20 overexpression, suggesting that the Hsp20 stimulatory effects are partially mediated through the PP1-PLN axis.

5. identification and characterization of a cardiac isoform of p20 associated with beta-adrenergic signaling in adult cardiomyocytes.

6. 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.

7. miR-320 is involved in the regulation of I/R-induced cardiac injury and dysfunction via antithetical regulation of Hsp20

8. Hsp20 expression prevents endotoxin-induced myocardial dysfunction and apoptosis via inhibition of NF-kappaB activation

9. Blockade of Hsp20 phosphorylation exacerbates cardiac ischemia/reperfusion injury by suppressed autophagy and increased cell death.

Xenopus laevis Heat Shock Protein, alpha-Crystallin-Related, B6 (HSPB6) Interaktionspartner

1. 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.

Cow (Bovine) Heat Shock Protein, alpha-Crystallin-Related, B6 (HSPB6) Interaktionspartner

1. HSP20 is associated with both actin and alpha-actinin; 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.

Zebrafish Heat Shock Protein, alpha-Crystallin-Related, B6 (HSPB6) Interaktionspartner

1. HSPB6 is expressed during development.