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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. De plus, nous expédions HSP90AA2 Protéines (6) et beaucoup plus de produits pour cette protéine.
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Human Polyclonal HSP90AA2 Primary Antibody pour ICC, IF - ABIN266969
Peterson, Moran, Conley, Bird: Zonal expression of endothelial nitric oxide synthase in sheep and rhesus adrenal cortex. dans Endocrinology 2001
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Human Monoclonal HSP90AA2 Primary Antibody pour IHC, ELISA - ABIN361714
Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. dans The Journal of biological chemistry 2003
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Human Monoclonal HSP90AA2 Primary Antibody pour ICC, IF - ABIN361663
Minami, Kawasaki, Miyata, Suzuki, Yahara: Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90. dans The Journal of biological chemistry 1991
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Human Polyclonal HSP90AA2 Primary Antibody pour 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. dans Developmental and comparative immunology 2013
Human Polyclonal HSP90AA2 Primary Antibody pour 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. dans Journal of leukocyte biology 2017
Knocking out Hsp90beta (Montrer HSP90AB1 Anticorps) leads to tumour cell death. Extracellular supplementation with recombinant Hsp90alpha, but not Hsp90beta (Montrer HSP90AB1 Anticorps), protein recovers tumourigenicity of the Hsp90alpha-knockout cells. Sequential mutagenesis identifies two evolutionarily conserved lysine residues, lys (Montrer LYZ Anticorps)-270 and lys (Montrer LYZ Anticorps)-277, in the Hsp90alpha subfamily that determine the extracellular Hsp90alpha function.
We revealed that Hsp90A (Montrer HSP90AA1 Anticorps) and Hsp90B (Montrer HSP90AB1 Anticorps) 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 (Montrer PRL Anticorps), cortisol, and ACTH (Montrer POMC Anticorps) 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 (Montrer CACNA1C Anticorps), HSP90alpha and corresponding decreased expression of HO-2 (Montrer HMOX2 Anticorps) in such hypoxic condition may play a protective role; to prevent cord blood RBC (Montrer CACNA1C Anticorps) against stress induced damage during preeclampsia.
STAT5b (Montrer STAT5B Anticorps) 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 (Montrer EGFR Anticorps) through TLR4 (Montrer TLR4 Anticorps) and a PKCdelta (Montrer PKCd Anticorps)/c-Src (Montrer SRC Anticorps) pathway, which induces ATP release and cytosolic Ca(2 (Montrer CA2 Anticorps)+) increase and finally favors glioblastoma cell migration.
High gene expression of Hsp90 alpha (Montrer HSP90AA1 Anticorps) 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.