Lane 1: Hela cell lysate
Lane 2: K562 cell lysate
Lane 3: Jurkat cell lysate
Lane 4: 293 cell lysate
Recombinant Rabbit monoclonal primary
Recombinant Hsp90 beta Monoclonal Antibody (ET1605-56)
Hela cell lysate, K562 cell lysate, Jurkat cell lysate, 293 cell lysate, Hela, HepG2, NIH/3T3, human liver carcinoma tissue, human colon carcinoma tissue, human breast carcinoma tissue, human tonsil tissue, mouse testis tissue, mouse brain tissue, Jurkat.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity 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.
The heat shock response was first described for Drosophila salivary gland cells and morphologically consists of a change in their polytene chromosome puffing patterns that involves de novo synthesis of a few proteins. Similar heat shock proteins were later discovered in bacterial chicken and mammalian cells, and have been subsequently studied in other organisms. A series of proteins including HSP 90, HSP 70, HSP 20-30 and ubiquitin are induced by insults such as temperature shock, chemicals and other environmental stress. A major function of HSP 90 and other HSPs is to act as molecular chaperones. HSP 90 forms a complex with glucocorticoid receptor (GR), rendering the non ligand-bound receptor transcriptionally inactive. HSP 90 binds the GR as a heterocomplex composed of either HSP 56 or Cyclophilin D, forming an aporeceptor comiplex. HSP 90 also exists as a dimer with other proteins such as p60/sti1 and p23, forming an apo-receptor complex with estrogen and androgen receptors.