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Human HSP90AA1 Protein expressed in Escherichia coli (E. coli) - ABIN2004288
Jakob: HSP90--news from the front. in Frontiers in bioscience : a journal and virtual library 2004
Show all 4 Pubmed References
Fusion of human SGT1 (show SUGT1 Proteins) (hSGT1 (show ECD Proteins)) to NOD1 (show NOD1 Proteins) LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha (show HSP90AA2 Proteins).
The major capsid protein of the mouse polyomavirus VP1 binds microtubules, HSP90 (show HSP90 Proteins), promotes their acetylation and blocks the host cell cycle.
Artificially maintaining Hsp90alpha (show HSP90AA2 Proteins) or knocking down Aarsd1L expression interferes with the differentiation of C2C12 myotubes.
Immune-mediated destruction of ovarian follicles associated with the presence of HSP90 (show HSP90 Proteins) antibodies.
identify that Hsp90alpha (show HSP90AA2 Proteins) at the transition neck region represents a signalling platform on which IRS-1 (show IRS1 Proteins) interacts with intracellular downstream signalling molecules involved in IGF-1 (show IGF1 Proteins) receptor signalling.
The study demonstrated that HSP90alpha plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells.
Data show that the heat shock protein 90 (HSP90 (show HSP90 Proteins)) isoforms HSP90AA1 and HSP90AB1 (show HSP90AB1 Proteins) are responsible for maintaining proper cellular levels of BMAL1 (show ARNTL Proteins) protein.
deficiency does not affect immunoglobulin gene hypermutation and class switch but causes enhanced MHC class II antigen presentation
study identified the essential role of Hsp90 (show HSP90 Proteins) in iNOS (show NOS2 Proteins) gene transactivation
Hsp90alpha (show HSP90AA2 Proteins) may be required to maintain and to activate these regulators and/or to disassemble the synaptonemal complex that holds homologous chromosomes together
FKBP51 (show FKBP4 Proteins) is primarily localized in mitochondria and hTERT is totally nuclear, upon the onset of oxidative stress, FKBP51 (show FKBP4 Proteins) (but not FKBP52 (show FKBP4 Proteins)) becomes mostly nuclear colocalizing with hTERT, and longer exposure times to peroxide favors hTERT export to mitochondria.
High HSP90 (show HSP90 Proteins) expression is associated with Colorectal Cancers.
High HSP90 (show HSP90 Proteins) expression is associated with prostate cancer.
Data suggest HSP90AA1-dependent regulation of ATM-NBN-CHK2 and ATR-CHK1 axes influences cells capability to repair double-stranded DNA damage; mechanisms include phosphorylation, polyubiquitination, and proteasomal degradation/proteolysis. (HSP90AA1 = heat shock protein 90kDa alpha; ATM = ataxia telangiectasia mutated protein; NBN = nibrin; CHK = checkpoint kinase; ATR = ataxia telangiectasia and Rad3 related kinase)
Data show that pyruvate kinase M2 (PKM2) directly interacted with mutant growth factor receptor (show RYK Proteins) (EGFR (show EGFR Proteins)) and heat-shock protein 90 (HSP90 (show HSP90 Proteins)), and thus stabilized EGFR (show EGFR Proteins) by maintaining its binding with HSP90 (show HSP90 Proteins) and co-chaperones.
Binding of FM807 to the N-terminus of Hsp90 (show HSP90 Proteins) disrupted Hsp90 (show HSP90 Proteins)/client complexes, resulting in degradation of the Hsp90 (show HSP90 Proteins) client protein EGFR (show EGFR Proteins) and inhibition of the downstream pathway.
Conventional as well as scaled molecular dynamics simulations further demonstrate that citrullination of selected Arg residues leads to progressive disruption of HSP90 tertiary structure, promoting exposure of R502/R510 to PAD modification and subsequent autoantibody binding.
SYK (show SYK Proteins) is an HSP90 (show HSP90 Proteins) client protein, and B-cell receptor signaling-dependent phosphorylation of HSP90 (show HSP90 Proteins) on Y197 is required for this interaction. HSP90 (show HSP90 Proteins) promotes Burkitt lymphoma cell survival by maintaining tonic B-cell receptor signaling.
There is overwhelming evidence that molecular chaperones such as Hsp27 (show HSPB1 Proteins), Hsp70 (show HSP70 Proteins) and Hsp90 (show HSP90 Proteins) are expressed at elevated levels in a wide range of cancers by stabilizing the mutated neoplasm proteins. (Review)
Data indicate a chaperone function of nicotinamide mononucleotide adenylyl transferase (show NMNAT1 Proteins) 2 (NMNAT2 (show NMNAT2 Proteins)), independent from its enzymatic activity, and NMNAT2 (show NMNAT2 Proteins) complexes with heat shock protein 90 (HSP90 (show HSP90 Proteins)) to refold aggregated protein substrates.
Feed intake remains low whereas respiratory frequency and body temperature remain higher and expression of HSP90 (show HSP90 Proteins), CAT1 (show SLC7A1 Proteins), SGLT1 (show SLC5A1 Proteins) and GLUT4 (show SLC2A4 Proteins) increases in some tissues in pigs under chronic heat stress conditions.
HSP90AA1 sperm content and the prediction of the boar ejaculate freezability.
Hsp90 (show HSP90 Proteins) is a modulator of eNOS (show NOS3 Proteins) activity and vascular reactivity in the newborn piglet pulmonary circulation
Apo (show C9orf3 Proteins)-Hsp90 (show HSP90 Proteins) is in a conformational equilibrium between two open states that have never been described previously.
Findings indicate an essential role for Hsp90 (show HSP90 Proteins) in nongenomic estrogen signaling in coronary artery smooth muscle cells.
Data suggest that elevated temperatures stimulate PGE2 production in ampullary oviduct by increasing expression of HSP90AA1 and PGES (prostaglandin-E synthase (show PTGES Proteins)).
This study showed that ubiquitinated ALK5 (show TGFBR1 Proteins) and phosphorylated heat shock protein 27 specifically accumulate in the cytoskeleton fraction, and ALK1 (show ACVRL1 Proteins) and ALK5 (show TGFBR1 Proteins) interact with heat shock protein 90(HSP90 (show HSP90 Proteins)).
The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene.
Heat Shock Protein 90, cytosolic
, heat shock protein 90A
, molecular chaperone
, HSP 86
, heat shock 86 kDa
, heat shock protein 1, alpha
, heat shock protein 90kDa alpha (cytosolic), class A member 1
, heat shock protein HSP 90-alpha
, heat shock protein, 1
, heat shock protein, 86 kDa 1
, heat shock protein, 89 kDa
, tumor-specific transplantation 86 kDa antigen
, heat shock protein 86
, epididymis luminal secretory protein 52
, heat shock 90kD protein 1, alpha
, heat shock 90kD protein 1, alpha-like 4
, heat shock 90kD protein, alpha-like 4
, heat shock 90kDa protein 1, alpha
, renal carcinoma antigen NY-REN-38
, heat shock protein HSP90 alpha
, hypothetical protein
, 90-kDa heat shock protein
, Heat shock protein HSP 90-alpha-like protein
, Hsp90 alpha
, heat shock protein 90 alpha
, heat shock protein 90kDa alpha, class A member 1