Immunoprecipitation (IP)
(Immunoprecipitation analysis using Mouse Anti-Hsp90 complex Monoclonal Antibody, Clone 8D3. Tissue: reticulocyte lysate. Species: Rabbit. Primary Antibody: Mouse Anti-Hsp90 complex Monoclonal Antibody at 1:1000. Hsp90 complex isolated by immunoprecipitation.)
Mouse Hsp90 Monoclonal Antibody | anti-HSP90AB1 antibody
Hsp90 complex Antibody: Alkaline Phosphatase
Immunoprecipitation (IP)
(Immunoprecipitation analysis using Mouse Anti-Hsp90 complex Monoclonal Antibody, Clone 8D3. Tissue: reticulocyte lysate. Species: Rabbit. Primary Antibody: Mouse Anti-Hsp90 complex Monoclonal Antibody at 1:1000. Hsp90 complex isolated by immunoprecipitation.)
Immunoprecipitation (IP)
(Immunoprecipitation analysis using Mouse Anti-Hsp90 complex Monoclonal Antibody, Clone 8D3. Tissue: reticulocyte lysate. Species: Rabbit. Primary Antibody: Mouse Anti-Hsp90 complex Monoclonal Antibody at 1:1000. Hsp90 complex isolated by immunoprecipitation.)
Scientific Background: Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (7).
1. Ardi, V.C., Alexander, L.D., Johnson, V. and McAlpine S.R. (2011). Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins. ACS Chem Biol. 6 (12), 1357-1366. doi: 10.1021/cb200203m
NCBI and Uniprot Product Information
NCBI Description
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]
Uniprot Description
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: signalosome; nucleoplasm; cell surface; mitochondrion; membrane; brush border membrane; basolateral plasma membrane; cytoplasm; apical plasma membrane; melanosome; inclusion body; cytosol
Molecular Function: protein binding; GTP binding; TPR domain binding; double-stranded RNA binding; unfolded protein binding; nitric-oxide synthase regulator activity; dATP binding; sulfonylurea receptor binding; protein kinase binding; kinase binding; ATP binding
Biological Process: axon guidance; positive regulation of nitric oxide biosynthetic process; positive regulation of cell size; positive regulation of protein import into nucleus, translocation; positive regulation of protein binding; protein folding; innate immune response; negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; response to salt stress; response to unfolded protein; placenta development
Research Articles on HSP90AB1
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Product Notes
The HSP90AB1 hsp90ab1 (Catalog #AAA800931) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The Hsp90 complex Antibody: Alkaline Phosphatase reacts with Human, Mouse, Rat, Rabbit and may cross-react with other species as described in the data sheet. AAA Biotech's Hsp90 can be used in a range of immunoassay formats including, but not limited to, Immunoprecipitation (IP). Best results for IP associated with use of goat anti-mouse IgM beads. Researchers should empirically determine the suitability of the HSP90AB1 hsp90ab1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "Hsp90, Monoclonal Antibody" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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