HSP90AA1 Protein, Pig, Recombinant (His)

HSP90AA1 Protein, Pig, Recombinant (His) is expressed in Baculovirus insect cells with N-6xHis tag. The predicted molecular weight is 19.7 kDa and the accession number is O02705.

规格	价格/CNY		货期	数量
20 μg	￥ 2,790	20日内发货
100 μg	￥ 7,840	20日内发货

规格

价格/CNY

货期

数量

20 μg

￥ 2,790

20日内发货

100 μg

￥ 7,840

20日内发货

产品描述	HSP90AA1 Protein, Pig, Recombinant (His) is expressed in Baculovirus insect cells with N-6xHis tag. The predicted molecular weight is 19.7 kDa and the accession number is O02705.

种属	Sus scrofa (Pig)
表达系统	Baculovirus Insect Cells
标签	N-6xHis
蛋白编号	O02705
氨基酸序列	VEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVR
蛋白构建	222-367 aa
蛋白纯度	> 90% as determined by SDS-PAGE.
分子量	19.7 kDa (predicted)

缓冲液	Tris-based buffer, 50% glycerol
复溶方法	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
存储	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
运输方式	In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
研究背景	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. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochodria outer membrane which promotes host antiviral response.

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HSP90AA1 Protein, Pig, Recombinant (His)

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