Hsp90 Beta (HSP90AB1) Antibody – Polyclonal

This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes. [provided by RefSeq, Dec 2012]

HSP90B: 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. Homodimer. Interacts with p53/TP53. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7. Interacts with FKBP4. Belongs to the heat shock protein 90 family.

Protein type: Heat shock protein; Chaperone

Chromosomal Location of Human Ortholog: 6p12

Cellular Component: apical plasma membrane; basolateral plasma membrane; brush border membrane; cell surface; cytoplasm; cytosol; inclusion body; melanosome; membrane; mitochondrion; nucleoplasm; signalosome

Molecular Function: ATP binding; dATP binding; double-stranded RNA binding; GTP binding; histone deacetylase binding; kinase binding; nitric-oxide synthase regulator activity; protein binding; protein kinase binding; protein kinase regulator activity; sulfonylurea receptor binding; TPR domain binding; unfolded protein binding

Biological Process: negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; placenta development; positive regulation of cell size; positive regulation of nitric oxide biosynthetic process; positive regulation of protein binding; positive regulation of protein import into nucleus, translocation; protein folding; protein stabilization; regulation of protein ubiquitination; response to salt stress; response to unfolded protein; virion attachment to host cell surface receptor