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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. Zusätzlich bieten wir Ihnen HSP90AA2 Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
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Human Monoclonal HSP90AA2 Primary Antibody für 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
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Human Monoclonal HSP90AA2 Primary Antibody für 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
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Human Polyclonal HSP90AA2 Primary Antibody für ICC, IF - ABIN266969
Peterson, Moran, Conley, Bird: Zonal expression of endothelial nitric oxide synthase in sheep and rhesus adrenal cortex. in Endocrinology 2001
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Human Monoclonal HSP90AA2 Primary Antibody für 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 für 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 (zeige AHSA1 Antikörper) and Hsp90 (zeige HSP90 Antikörper) promote severe craniofacial phenotypes in zebrafish model of HDR (zeige GATA3 Antikörper) syndrome.
Perturbation of the HSP70 (zeige HSPA1A Antikörper)-HSP90 (zeige HSP90 Antikörper) heat-shock protein axis stimulates degradation of endothelial VEGFR2 (zeige KDR Antikörper).
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 (zeige HSP90 Antikörper) 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 (zeige UNC45B Antikörper) interacts with the chaperone Hsp90a (zeige HSP90AA1 Antikörper) in vitro. The two genes are co-expressed in the skeletal musculature.
Embryonic heat shock reveals latent hsp90 (zeige HSP90 Antikörper) translation in zebrafish.
Loss of Hsp90a (zeige HSP90AA1 Antikörper) function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a (zeige HSP90AA1 Antikörper) and several other genes encoding proteins that may act with Hsp90a (zeige HSP90AA1 Antikörper) 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 (zeige HSP90AB1 Antikörper) leads to tumour cell death. Extracellular supplementation with recombinant Hsp90alpha, but not Hsp90beta (zeige HSP90AB1 Antikörper), protein recovers tumourigenicity of the Hsp90alpha-knockout cells. Sequential mutagenesis identifies two evolutionarily conserved lysine residues, lys (zeige LYZ Antikörper)-270 and lys (zeige LYZ Antikörper)-277, in the Hsp90alpha subfamily that determine the extracellular Hsp90alpha function.
We revealed that Hsp90A (zeige HSP90AA1 Antikörper) and Hsp90B (zeige HSP90AB1 Antikörper) are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.
Heat shock protein 90 (zeige HSP90 Antikörper) stimulates rat mesenchymal stem cell migration via PI3K (zeige PIK3CA Antikörper)/Akt (zeige AKT1 Antikörper) and ERK1/2 (zeige MAPK1/3 Antikörper) pathways
Studied the serum prolactin (zeige PRL Antikörper), cortisol, and ACTH (zeige POMC Antikörper) 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 (zeige CACNA1C Antikörper), HSP90alpha and corresponding decreased expression of HO-2 (zeige HMOX2 Antikörper) in such hypoxic condition may play a protective role; to prevent cord blood RBC (zeige CACNA1C Antikörper) against stress induced damage during preeclampsia.
STAT5b (zeige STAT5B Antikörper) 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 (zeige EGFR Antikörper) through TLR4 (zeige TLR4 Antikörper) and a PKCdelta (zeige PKCd Antikörper)/c-Src (zeige SRC Antikörper) pathway, which induces ATP release and cytosolic Ca(2 (zeige CA2 Antikörper)+) increase and finally favors glioblastoma cell migration.
High gene expression of Hsp90 alpha (zeige HSP90AA1 Antikörper) 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