| Form | Liquid |
|---|---|
| Host Species | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Purification | Purified by antigen affinity column. |
| Endotoxin Level | Please contact with the lab for this information. |
| Applications | ELISA, IHC, WB |
| Species Reactivity | Mouse, Human, Rat, Horse |
| Target | HSP 84, HSP 90, HSP84, HSP90AB1, HSP90B, HSPC2, HSPC3, HSPCB, Heat shock 84 kDa, Heat shock protein HSP 90-beta, Heat shock protein family C member 3 |
| Immunogen | E. coli - derived recombinant Human HSP90AB1 (Met1-Asp724). |
| Storage Buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping Condition | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Product Usage Information | ELISA: 1:2000-1:20000; WB: 1:500-1:2000 |
| Accession Number | P08238 |
| Background | Heat shock protein HSP 90-beta (HSP90AB1) is a ~83 kDa protein. 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 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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. 1. Chadli, A. et al. (2006) Molecular and cellular biology 26, 1722-30. PMID: 16478993 2. Retzlaff, M. et al. (2009) EMBO reports 10, 1147-53. PMID: 19696785 3. Pearl, LH. (2016) Biopolymers 105, 594-607. PMID: 26991466 4. Verma, S. et al. (2016) Biochimie 127, 227-40. PMID: 27295069 5. Khurana, N. et al. (2015) Frontiers in oncology 5, 100. PMID: 25973397 6. Shang, Y. et al. (2014) Biochemical and biophysical research communications 446, 387-92. PMID: 24613385 7. Didelot, C. et al. (2008) Cell death and differentiation 15, 859-66. PMID: 18239673 8. Cheng, MB. et al. (2010) Cellular signalling 22, 1206-13. PMID: 20353823 9. Zhang, M. et al. (2020) Cell 181, 637-652.e15. PMID: 32272059 |
| Note | For research use only |
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|---|---|
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