HSP90AB1 Antibody – Rabbit 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: Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 6p12

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

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

Biological Process: axon guidance; positive regulation of nitric oxide biosynthetic process; protein folding; positive regulation of cell size; positive regulation of protein import into nucleus, translocation; positive regulation of protein binding; innate immune response; negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; response to unfolded protein; response to salt stress; placenta development