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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. Additionally we are shipping HSP90AA2 Proteins (6) and many more products for this protein.
Showing 10 out of 212 products:
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
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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
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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
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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
Human Polyclonal HSP90AA2 Primary Antibody for ICC, IF - ABIN4320479
Bzowska, Nogieć, Bania, Zygmunt, Zarębski, Dobrucki, Guzik: Involvement of cell surface 90 kDa heat shock protein (HSP90) in pattern recognition by human monocyte-derived macrophages. in Journal of leukocyte biology 2017
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 stimulates rat mesenchymal stem cell migration via PI3K/Akt and ERK1/2 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.