Recombinant Human HSP90AB1 Protein, N-His (PX-P5753)
概述
图片
参考文献
概述
货号
PX-P5753
品牌
ProteoGenix
描述
Recombinant Human HSP90AB1 Protein, N-His (PX-P5753) expressed in E. coli, Purity: >90% as determined by SDS-PAGE..
Highlights
High Purity (>90% as determined by SDS-PAGE.) — Verified by SDS-PAGE for downstream accuracy.
E. coli Expression — Optimized for functional studies.
表达系统
E. coli
Accession号
P08238
蛋白长度
Met1-Asp724
应用
ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
种属
Homo sapiens (Human)
性质
Recombinant
内毒素水平
Please contact with the lab for this information.
纯度
>90% as determined by SDS-PAGE.
预测分子量
85.57 kDa
状态
Lyophilized
保存溶液
Lyophilized from a solution in PBS pH 7.4, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
重悬
Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
运输
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
稳定性和存储
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.
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
