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Product Search Results: SPR-102B

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Product Search Results: SPR-102B

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StressMarq SPR-102B 100 µg £224.00
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Background Info: 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
Product Type: Protein
Format: 20mM Tris, pH7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT
Storage Temp: -20ºC
Species Reactivity: Hu
Applications: WB | SDS-PAGE | Functional Assay | ELISA | Co-IP | Surface Plasmon Resonance (SPR)
Research Area(s): Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers
Target: HSP90 beta
Conjugate: No tag
Alternative Name(s): FLJ26984 Protein, HSP84 Protein, HSP90 Protein, HSP90B Protein, HSPC2 Protein, HSPCB Protein
Category: Recombinant
Accession Number: NP_031381.2
Gene ID: 3326
Swiss-Prot: P08238
Species Reactivity Full Name: Human
Purification: Affinity Purified | Endotoxin-free
Concentration: Lot/batch specific. See included datasheet.
Specificity: ~90 kDa
Certificate of Analysis: This product has been certified >90% pure using SDS-PAGE analysis.
Cellular Localization: Cytoplasm | Melanosome
References: 1. Arlander S.J.H., et al. (2003) J Biol Chem. 278: 52572-52577.
2. Pearl H., et al. (2001) Adv Protein Chem. 59:157-186.
3. Neckers L., et al. (2002) Trends Mol Med. 8:S55-S61.
4. Pratt W., Toft D. (2003) Exp Biol Med. 228:111-133.
5. Pratt W., Toft D. (1997) Endocr Rev. 18: 306–360.
6. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420–434.
7. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 8324– 8328.
Tarriff Code: 3822.00.1090
ADR Code: Non-hazardous
UN Code for transport: Non-hazardous
Country of Origin: Canada
Cite this Product: Human Recombinant HSP90 beta Protein (StressMarq Biosciences, Canada, Cat # SPR-102B)
Biological Activity: ATPase active
Biological Activity Abreviation: Active
Expression System: Baculovirus/Hi5 cells
Protein Length: Full Length
Purity: >90%
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.