Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
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. Additionally we are shipping HSP90AA2 Proteins (6) and many more products for this protein.
Showing 10 out of 158 products:
Human Monoclonal HSP90AA2 Primary Antibody for IHC, ELISA - ABIN361714
Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. in The Journal of biological chemistry 2003
Show all 16 references for 361714
Human Monoclonal HSP90AA2 Primary Antibody for ICC, IF - ABIN361663
Minami, Kawasaki, Miyata, Suzuki, Yahara: Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90. in The Journal of biological chemistry 1991
Show all 15 references for 361663
Human Polyclonal HSP90AA2 Primary Antibody for ICC, IF - ABIN266969
Peterson, Moran, Conley, Bird: Zonal expression of endothelial nitric oxide synthase in sheep and rhesus adrenal cortex. in Endocrinology 2001
Show all 7 references for 266969
Human Monoclonal HSP90AA2 Primary Antibody for ICC, IF - ABIN2481730
Pearl, Prodromou: Structure, function, and mechanism of the Hsp90 molecular chaperone. in Advances in protein chemistry 2002
Human Polyclonal HSP90AA2 Primary Antibody for IF (p), IHC (p) - ABIN1714199
Ding, Wu, Su, Zhou, Zhao, Deng, Zhang, Liu, Wang, Liu: Expression of heat shock protein 90 genes during early development and infection in Megalobrama amblycephala and evidence for adaptive evolution in teleost. in Developmental and comparative immunology 2013
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.
Knocking out Hsp90beta (show HSP90AB1 Antibodies) leads to tumour cell death. Extracellular supplementation with recombinant Hsp90alpha, but not Hsp90beta (show HSP90AB1 Antibodies), protein recovers tumourigenicity of the Hsp90alpha-knockout cells. Sequential mutagenesis identifies two evolutionarily conserved lysine residues, lys (show LYZ Antibodies)-270 and lys (show LYZ Antibodies)-277, in the Hsp90alpha subfamily that determine the extracellular Hsp90alpha function.
We revealed that Hsp90A (show HSP90AA1 Antibodies) and Hsp90B (show HSP90AB1 Antibodies) are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.
Heat shock protein 90 (show HSP90 Antibodies) stimulates rat mesenchymal stem cell migration via PI3K (show PIK3CA Antibodies)/Akt (show AKT1 Antibodies) and ERK1/2 (show MAPK1/3 Antibodies) pathways
Studied the serum prolactin (show PRL Antibodies), cortisol, and ACTH (show POMC Antibodies) stress response of intensive care unit (ICU) patients with severe sepsis/septic shock (SS) or systemic inflammatory response syndrome (SIRS) compared to healthy subjects.
These results indicate that cytoplasmic HSP90alpha may serve as a biomarker for perineural invasion in pancreatic cancer
Increased expression of nucleated RBC (show CACNA1C Antibodies), HSP90alpha and corresponding decreased expression of HO-2 (show HMOX2 Antibodies) in such hypoxic condition may play a protective role; to prevent cord blood RBC (show CACNA1C Antibodies) against stress induced damage during preeclampsia.
STAT5b (show STAT5B Antibodies) pathway regulates Hsp90alpha expression under hypoxic conditions
HSP90alpha was an IMH-2 epitope-associated protein. Tumor HSP90alpha overexpression was correlated with the metastasis and poor prognosis of colorectal cancer patients.
extracellular HSP90alpha transactivates EGFR/ErbB1 (show EGFR Antibodies) through TLR4 (show TLR4 Antibodies) and a PKCdelta (show PKCd Antibodies)/c-Src (show SRC Antibodies) pathway, which induces ATP release and cytosolic Ca(2 (show CA2 Antibodies)+) increase and finally favors glioblastoma cell migration.
High gene expression of Hsp90 alpha (show HSP90AA1 Antibodies) is associated with leukemia.
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