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Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction.
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Zebrafish Polyclonal HSP90AA1.1 Primary Antibody for WB - ABIN1945096
Lele, Hartson, Martin, Whitesell, Matts, Krone: Disruption of zebrafish somite development by pharmacologic inhibition of Hsp90. in Developmental biology 1999
Show all 5 Pubmed References
The transcriptional up-regulation of unc45b, hsp90aa1.1 and smyd1b is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models
Data indicate that heat shock protein 90alpha (Hsp90alpha1) function in myosin thick filament organization is potentially regulated by post-translational modification (PTM) involving phosphorylation and acetylation.
The chaperone proteins Ahsa1 (show AHSA1 Antibodies) and Hsp90 (show HSP90 Antibodies) promote severe craniofacial phenotypes in zebrafish model of HDR (show GATA3 Antibodies) syndrome.
Perturbation of the HSP70 (show HSPA1A Antibodies)-HSP90 (show HSP90 Antibodies) heat-shock protein axis stimulates degradation of endothelial VEGFR2 (show KDR Antibodies).
studies indicate that the hsp90alpha1 mutant phenotype is not simply due to disruption of myosin folding and assembly, suggesting that Hsp90alpha1 may play a role in the assembly and organization of other sarcomeric structures
Mild perturbation of Hsp90 (show HSP90 Antibodies) function at critical developmental stages may underpin the variable penetrance and expressivity of many developmental anomalies where the interaction between genotype and environment plays a major role.
Steif/Unc-45b (show UNC45B Antibodies) interacts with the chaperone Hsp90a (show HSP90AA1 Antibodies) in vitro. The two genes are co-expressed in the skeletal musculature.
Embryonic heat shock reveals latent hsp90 (show HSP90 Antibodies) translation in zebrafish.
Loss of Hsp90a (show HSP90AA1 Antibodies) function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a (show HSP90AA1 Antibodies) and several other genes encoding proteins that may act with Hsp90a (show HSP90AA1 Antibodies) during sarcomere assembly.
In response to stress or damage to the myofiber, Unc45b and Hsp90a dissociate from the Z line and transiently associate with myosin.
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.
, heat shock protein 90-alpha 1
, heat shock protein HSP 90-alpha 1