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Anti-Human HSP90AB1 Polyclonal Antibody (HY418014)

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Overview
Catalog No.HY418014
Description
Anti-Human HSP90AB1 Polyclonal Antibody (HY418014) is a rabbit polyclonal antibody detecting HSP90AB1. Suitable for Mouse, Human, and Rat.
Highlights
  • Multi-Species — Cross-reactive for translational research.
Species reactivityHuman, Mouse, Rat
ApplicationsELISA, IHC, WB
Host speciesRabbit
IsotypeIgG
Clonality Polyclonal
Immunogen E. coli - derived recombinant Human HSP90AB1 (Met1-Asp724).
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
Endotoxin level Please contact with the lab for this information.
Purification Purified by antigen affinity column.
Accession P08238
Form Liquid
Storage buffer 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

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 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
Application Dilution
ELISA 1:2000-1:20000
WB 1:500-1:2000
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.
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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Formula
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