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In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. Additionally we are shipping HSPA6 Antibodies (65) and HSPA6 Kits (3) and many more products for this protein.
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endothelial nitric oxide synthase (show NOS3 Proteins) induces heat shock protein HSPA6 (HSP70B') in human arterial smooth muscle cells
High BCLC staging scores, advanced cirrhosis and the overexpression of HSPA12A and HSP90B1 (show HSP90B1 Proteins) might be associated with poor survival from HCC (show FAM126A Proteins), whereas high levels of HSPA4 (show HSPA4 Proteins), HSPA5 (show HSPA5 Proteins) and HSPA6 might be associated with earlier recurrence of HCC (show FAM126A Proteins)
Data indicate that heat shock protein 90kD(HSP90 (show HSP90 Proteins)) inhibition induces heat shock 70kD protein 6 (HSP70B') expression.
Potential stress-sensitive sites were identified in differentiated human SH-SY5Y cells by the localization of HSPA6 (HSP70B') and HSPA1A (HSP70-1 (show HSPA1A Proteins)) to nuclear components following heat shock
HSPA6 regulation by TNIP1 (show TNIP1 Proteins) occurs in promoter regions lacking binding sites for known TNIP1 (show TNIP1 Proteins)-repressed transcription factors
Following a brief period of thermal stress, YFP-tagged HSPA6 and HSPA1A (show HSPA1A Proteins) rapidly appeared at centrioles in the cytoplasm of human neuronal cells.
Hsp70B' also formed complexes with Hsp40 (show DNAJB1 Proteins) suggesting a common co-chaperone for HSP70 (show HSP70 Proteins) family members.
Heat shock protein 70B' (HSP70B') expression and release in response to human oxidized low density lipoprotein immune complexes in macrophages.
These findings are likely to be important in pathological conditions in which Hsp70B' contributes to cell survival.
Hsp70B' expressed on colon cells after proteasome inhibition was most closely related to Hsp72 (show HSPA1A Proteins). They shared 100% AA identity in the peptide-binding region but differed in the lid and C-terminal domains.Hsp70B' appeared to have diverged recently.
There was a significant decrease in the systemic HSP70 (show HSP70 Proteins) levels of trauma groups (moderate and severe hemorrhage) when compared to the sham trauma group, which was significantly decreased compared to baseline values in severe hemorrhage over the entire time course.
Host HSP70 and Classical swine fever virus NS5A protein complex formation is confirmed by coimmunoprecipitation and GST-pulldown studies.
This study evaluated the expression of 70kDa (show RPS6KB1 Proteins) heat shock proteins and the concentration of thiobarbituric acid reactive substances and nitric oxide ions as markers of oxidative stress in swine.
This study revealed that HSP70 (show HSP70 Proteins) is an essential host factor required for the replication of porcine reproductive and respiratory syndrome virus.
A specific interaction between Hsp70 and porcine circovirus type 2 Cap (capsid protein) was confirmed by colocalization by confocal microscopy and co-immunoprecipitation.
This work investigated the expression of heat shock protein 70 (show HSP70 Proteins) by Western blot in swine liver. Animals in an intensive/indoor confinement system showed significantly higher HSP70 (show HSP70 Proteins) values compared with those in an extensive/outdoor system.
The results indicate that Heat shock protein 70 (Hsp70) mediates distinct stress-related functions in different tissues during transportation. Heat shock factor-1 (HSF-1) levels were reduced at 1 and 4 h only in the hearts of transported pigs.
These results indicated that the expression of Hsp70 (show HSP70 Proteins) in the intestinal piglets was upregulated by IUGR, and different intestinal sites had different responses to stress.
Induction of tolerance to heat shock correlated with the induced expression of heat shock protein 70 (show HSP70 Proteins). HSP70 (show HSP70 Proteins) and compatible osmolytes have distinct roles in cellular adaptation to these stresses.
HSP-70 (show HSP70 Proteins) is an endogenous protectant of which its actions may be unmasked and/or potentiated with exogenous administration before brain injury
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).
heat shock 70kDa protein 6 (HSP70B')
, heat shock 70kD protein 4 *(human-HSPA6)
, heat shock 70 kDa protein 6
, heat shock 70 kDa protein B'
, heat shock 70kD protein 6 (HSP70B')
, Heat shock 70 kDa protein 6
, heat shock 70 kDa protein