Anti-HSP90AA1 Polyclonal Antibody (HY503014)

Name: Anti-HSP90AA1 Polyclonal Antibody
Brand: abinScience
SKU: HY503014
Price: 96 USD
Availability: InStock

Datasheet Share product Copy info

Price(USD):

Spec:

20ug
50ug
100ug

Number:

Get quote

Overview
Images
References
Datasheet
SDS

Overview

Catalog No.

HY503014

Species reactivity

Human, Mouse, Rat

Applications

ELISA, IHC, WB

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Immunogen

E. coli - derived recombinant Human HSP90AA1 (Ser39-Asp193).

Target

LPS-associated protein 2, Heat shock protein HSP 90-alpha, HSPCA, HSP90A, HSP 86, Lipopolysaccharide-associated protein 2, HSP86, HSP90AA1, Heat shock 86 kDa, Renal carcinoma antigen NY-REN-38, LAP-2, HSPC1

Purification

Purified by antigen affinity column.

Accession

P07900

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.

Product Usage Information

Application	Dilution
ELISA	1:5000-1:20000
IHC	1:50-1:500
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-alpha (HSP90AA1) is a ~84 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 that is linked to its ATPase activity which is essential for its chaperone 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. Forsythe, HL. et al. (2001) The Journal of biological chemistry 276, 15571-4. PMID: 11274138

2. Young, JC. et al. (2003) Cell 112, 41-50. PMID: 12526792

3. Yang, J. et al. (2005) The EMBO journal 24, 1-10. PMID: 15577939

4. Martínez-Ruiz, A. et al. (2005) Proceedings of the National Academy of Sciences of the United States of America 102, 8525-30. PMID: 15937123

5. Woodford, MR. et al. (2016) Nature communications 7, 12037. PMID: 27353360

6. Woodford, MR. et al. (2017) The EMBO journal 36, 3650-3665. PMID: 29127155

7. Pearl, LH. (2016) Biopolymers 105, 594-607. PMID: 26991466

8. Verma, S. et al. (2016) Biochimie 127, 227-40. PMID: 27295069

9. Khurana, N. et al. (2015) Frontiers in oncology 5, 100. PMID: 25973397

10. Triantafilou, K. et al. (2001) Nature immunology 2, 338-45. PMID: 11276205

Note

For research use only.

Images

Western blot

Western blot analysis was performed using anti-HSP90AA1 polyclonal antibody at 1µg/ml on various samples.
Lane 1: NIH3T3 cell lysate
Lane 2: PC-12 cell lysate
Lane 3: Hela cell lysate
Lane 4: MCF-7 cell lysate
Lane 5: Jurkat cell lysate
Lane 6: Lncap cell lysate
Lane 7: Raji cell lysate
Lane 8: Mouse brain lysate
Lane 9: Rat brain lysate