HSP90AB1 antibody (APC)
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- Target See all HSP90AB1 Antibodies
- HSP90AB1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1))
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Reactivity
- Human
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Host
- Rabbit
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Clonality
- Polyclonal
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Conjugate
- This HSP90AB1 antibody is conjugated to APC
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Application
- Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)
- Specificity
- Detects ~90kda. Does not cross-react with HSP90α.
- Cross-Reactivity
- Human, Mouse, Rat
- Purification
- Peptide Affinity Purified
- Immunogen
- Full length protein HSP90
- Top Product
- Discover our top product HSP90AB1 Primary Antibody
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- Application Notes
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- WB (1:1000)
- IHC (1:100)
- ICC/IF (1:120)
- optimal dilutions for assays should be determined by the user.
- Comment
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A 1:1000 dilution of ABIN2486706 was sufficient for detection of HSP90 in 20 μg of HeLa cell lysate by ECL immunoblot analysis.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
- Preservative
- Sodium azide
- Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Storage
- 4 °C
- Storage Comment
- Conjugated antibodies should be stored at 4°C
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- Target
- HSP90AB1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1))
- Alternative Name
- HSP90 beta (HSP90AB1 Products)
- 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
- Gene ID
- 3326
- NCBI Accession
- NP_031381
- UniProt
- P08238
- Pathways
- Regulation of Cell Size
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