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AB318253

重组人HSP90 alpha蛋白(His-tag)

Recombinant Human HSP90 alpha Protein (His-tag)

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Recombinant Human HSP90 alpha Protein (His-tag) is a Human Full Length protein, in the 1 to 732 aa range, expressed in Escherichia coli, with <95%, <0.005 EU/µg endotoxin level, suitable for Mass Spec, SDS-PAGE.

查看别名

HSP90A, HSPC1, HSPCA, HSP90AA1, Heat shock protein HSP 90-alpha, Heat shock 86 kDa, Heat shock protein family C member 1, Lipopolysaccharide-associated protein 2, Renal carcinoma antigen NY-REN-38, HSP 86, HSP86, LAP-2, LPS-associated protein 2

2 Images
Mass Spectrometry - Recombinant Human HSP90 alpha Protein (His-tag) (AB318253)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human HSP90 alpha Protein (His-tag) (AB318253)

Mass determination by ESI-TOF. Predicted MW is 85720.00 Da (+/- 10 Da by ESI-TOF). Observed MW is 85592.99 Da.

SDS-PAGE - Recombinant Human HSP90 alpha Protein (His-tag) (AB318253)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human HSP90 alpha Protein (His-tag) (AB318253)

SDS-PAGE analysis of ab318253 under reducing conditions for 2ug protein.

关键信息

纯度

<95% HPLC

内毒素水平

<0.005 EU/µg

表达系统

Escherichia coli

标签

His tag C-Terminus

应用

Mass Spec, SDS-PAGE

applications

生物活性

No

质谱

LC-MS/MS

访问

P07900

不含动物源

Yes

不含载体蛋白

No

种属

Human

存储溶液

pH: 7.4 Constituents: PBS, 10% Glycerol (glycerin, glycerine)

storage-buffer

反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

序列信息

[{"sequence":"MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD","proteinLength":"Full Length","predictedMolecularWeight":"85.72 kDa","actualMolecularWeight":"85.6 kDa","aminoAcidEnd":732,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P07900","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

性能和储存信息

运输条件
Dry Ice
推荐的短期储存条件
-80°C
推荐的长期储存条件
-80°C
False

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

Hsp90 alpha also known as Hsp90AA1 or 5G5 is a molecular chaperone with an approximate molecular weight of 90 kDa. It plays an important role in the folding stability and function of many client proteins. This protein is expressed ubiquitously in eukaryotic cells with high levels in the cytoplasm and the endoplasmic reticulum. Hsp90 alpha operates through a unique ATPase-driven chaperone cycle that modulates protein conformations helping in the assembly and disassembly of protein complexes.
Biological function summary

Hsp90 alpha assists in maintaining protein homeostasis and is part of a larger chaperome complex including co-chaperones and other chaperones such as Hsp70. It plays an important role in stress response by stabilizing proteins and preventing aggregation. Hsp90 alpha is essential for the normal function of several kinases and transcription factors which are important for cell signaling and regulation processes. It functions as a mediator for cellular response to environmental cues.

Pathways

Hsp90 alpha is an integral component in the signal transduction and cell cycle control pathways. It interacts with various signaling proteins and receptors like AKT and steroid hormone receptors to facilitate their proper folding and activation. Furthermore Hsp90 alpha influences the MAPK/ERK pathway playing a role in cell proliferation and differentiation. Its interaction with Hsp90 protein clients creates a regulatory framework across multiple pathways allowing precise control over cellular function.

Hsp90 alpha is linked to cancer and neurodegenerative diseases. Its enhanced expression in tumors correlates with the stabilization of oncogenic client proteins such as HER2 contributing to cancer progression. Additionally Hsp90 alpha relates to disorders like Alzheimer's disease due to its role in handling misfolded proteins. The protein interacts with co-chaperones like H1L1 which may influence its impact on disease outcomes highlighting the therapeutic potential of targeting Hsp90 alpha in these conditions.

特殊说明

形式

Liquid

常规信息

功能

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 (PubMed : 11274138, PubMed : 12526792, PubMed : 15577939, PubMed : 15937123, PubMed : 27353360, PubMed : 29127155). 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 (PubMed : 29127155). 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 (PubMed : 26991466, PubMed : 27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed : 12526792). 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 (PubMed : 25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed : 25973397). 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 (PubMed : 25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed : 25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed : 11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed : 24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed : 20628368, PubMed : 25609812).. (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion.

序列相似性

Belongs to the heat shock protein 90 family.

翻译后修饰

ISGylated.. S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.. Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways.

亚细胞定位

Nucleus

产品实验方案

靶点信息

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 (PubMed : 11274138, PubMed : 12526792, PubMed : 15577939, PubMed : 15937123, PubMed : 27353360, PubMed : 29127155). 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 (PubMed : 29127155). 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 (PubMed : 26991466, PubMed : 27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed : 12526792). 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 (PubMed : 25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed : 25973397). 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 (PubMed : 25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed : 25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed : 11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed : 24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed : 20628368, PubMed : 25609812).. (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion.
See full target information HSP90AA1

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