Lane 1: Hela
Lane 2: NIH/3T3
Lane 3: PC12
Lane 4: 293T
Lane 5: HePG2
Lane 6: COS-1
Lane 7: Jurkat
Lane 8: A549
Lane 9: Raji
Lane 10: Mouse heart tissue
Mouse monoclonal primary
HSP90 Beta Monoclonal Antibody (EM21103)
Hela, NIH/3T3, PC12, 293T, A431, COS-1, Jurkat, HepG2, A549, Raji, mouse brain tissue, mouse heart tissue, rat brain tissue , rat heart tissue,human colon carcinoma tissue,human tonsil tissue,mouse testis tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
90 kda heat shock protein beta HSP90 beta antibody; D6S182 antibody; FLJ26984 antibody; Heat shock 84 kDa antibody; Heat shock 90kD protein 1, beta antibody; Heat shock 90kDa protein 1 beta antibody; Heat shock protein 90 alpha family class B member 1 antibody; Heat shock protein 90 kDa antibody; Heat shock protein 90kDa alpha (cytosolic) class B member 1 antibody; Heat shock protein 90kDa alpha family class B member 1 antibody; Heat shock protein beta antibody; Heat shock protein HSP 90 beta antibody; Heat shock protein HSP 90-beta antibody; HS90B_HUMAN antibody; HSP 84 antibody; HSP 90 antibody; HSP 90 b antibody; HSP 90b antibody; HSP84 antibody; HSP90 BETA antibody; hsp90ab1 antibody; HSP90B antibody; HSPC2 antibody; HSPCB antibody
Belongs to the heat shock protein 90 family.
Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).; ISGylated.; S-nitrosylated; negatively regulates the ATPase activity.; Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.; Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation.; Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins.
Hsp90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. Two isoforms which correspond to the major and minor isoform , (Hsp90 α and Hsp90 β ) can be found in nearly equal amount in humans, and operates as part of a multichaperone machinery in the cytosol, which includes Hsp70, peptidyl-prolyl isomerases and other cochaperones.