Anti-GRP94/HSP90B1 Antibody Picoband® Fluoro488 Conjugated

Heat shock protein 90kDa beta member 1  (HSP90B1), known also as  endoplasmin, GRP94, is a chaperone protein  that in humans is encoded by the  HSP90B1  gene. It is mapped to chromosome 12q23.3. This gene encodes a member of a family of adenosine triphosphate (ATP) -metabolizing molecular chaperones with roles in stabilizing and folding other proteins. The encoded protein is localized to melanosomes and the endoplasmic reticulum. Expression of this protein is associated with a variety of pathogenic states, including tumor formation.

Endoplasmin;94 kDa glucose-regulated protein; GRP-94; Heat shock protein 90 kDa beta member 1; Tumor rejection antigen 1; gp96 homolog; HSP90B1; GRP94, TRA1

Most abundant in testis, slightly less abundant in skeletal muscle and heart, followed by prostate, thymus, ovary, small intestine, and colon. Not detected in the peripheral blood leukocytes.

Cancer, Cancer Metabolism, ER Proteins, Metabolism, Metabolism Processes, Organelles, Pathways and Processes, Protein Trafficking, Response To Hypoxia, Signal Transduction, Subcellular Markers, Tags & Cell Markers

Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity) . Functions in endoplasmic reticulum associated degradation (ERAD) . Has ATPase activity. .

1. Rebbe NF, Hickman WS, Ley TJ, Stafford DW, Hickman S (Oct 1989) . Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene. J Biol Chem 264 (25) : 15006–11. 2. Chen B, Piel WH, Gui L, Bruford E, Monteiro A (Dec 2005) . The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86 (6) : 627–37. 3. Entrez Gene: HSP90AB1 Heat shock protein 90kDa alpha (cytosolic), class B member 4. Chen, B., Piel, W. H., Gui, L., Bruford, E., Monteiro, A. The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86: 627-637, 2005. 5. Prodromou C, Panaretou B, Chohan S, Siligardi G, O'Brien R, Ladbury JE, Roe SM, Piper PW, Pearl LH (August 2000) . The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J. 19 (16) : 4383–92.