Glucose Regulated Protein 94 (HSP90B1) Antibody – Goat Polyclonal

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]

GRP94: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9. Interacts with CNPY3. This interaction is disrupted in the presence of ATP. Interacts with TLR4 and TLR9, but not with TLR3. Belongs to the heat shock protein 90 family.

Protein type: Secreted; Heat shock protein; Apoptosis; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 12q24.2-q24.3

Cellular Component: endoplasmic reticulum membrane; focal adhesion; endoplasmic reticulum; endoplasmic reticulum lumen; extracellular region; cytosol; extracellular matrix; membrane; perinuclear region of cytoplasm; melanosome; plasma membrane; midbody; nucleus

Molecular Function: protein binding; low-density lipoprotein receptor binding; RNA binding; unfolded protein binding; virion binding; calcium ion binding; protein phosphatase binding; ATP binding

Biological Process: actin rod formation; receptor-mediated endocytosis; ER-associated protein catabolic process; unfolded protein response; regulation of phosphoprotein phosphatase activity; protein transport; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; sequestering of calcium ion; response to hypoxia; toll-like receptor signaling pathway; innate immune response; negative regulation of apoptosis