HSP90AA1 Protein, Human (His-SUMO)

The HSP90AA1 protein is an important molecular chaperone that coordinates the maturation and regulation of specific target proteins critical for cell cycle control and signal transduction. Its ATPase activity drives a functional cycle that induces conformational changes in client proteins for activation. HSP90AA1 Protein, Human (His-SUMO) is the recombinant human-derived HSP90AA1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of HSP90AA1 Protein, Human (His-SUMO) is 224 a.a., with molecular weight of ~43 kDa.

HSP90AA1 protein, a molecular chaperone, plays a crucial role in the maturation, structural maintenance, and regulation of specific target proteins involved in cell cycle control and signal transduction. Operating through a functional cycle linked to its ATPase activity, essential for its chaperone function, HSP90AA1 induces conformational changes in client proteins, activating them. Dynamic interactions with co-chaperones modulate substrate recognition, the ATPase cycle, and chaperone function. Engaging with diverse client protein classes through co-chaperones, it forms functional chaperones that release properly folded client proteins and co-chaperones in an ADP-bound partially open conformation. Apart from its chaperone activity, HSP90AA1 plays a critical role in mitochondrial import by delivering preproteins to the mitochondrial import receptor TOMM70. It also contributes to the regulation of the transcription machinery at multiple levels, altering transcription factor levels, modulating epigenetic modifiers, and participating in histone eviction from gene promoters. Furthermore, HSP90AA1 binds bacterial lipopolysaccharide, mediating LPS-induced inflammatory responses, including TNF secretion. It antagonizes STUB1-mediated inhibition of TGF-beta signaling and facilitates the association of TOMM70 with IRF3 or TBK1 in the mitochondrial outer membrane, promoting host antiviral responses. In the context of microbial infection, HSP90AA1 interferes with N.meningitidis NadA-mediated invasion of human cells, influencing the adhesion and entry of E.coli expressing NadA into human Chang cells based on its expression levels.

Data is not available.

Human

E. coli

N-6*His;N-SUMO

P07900 (D9-D232)

3320  [NCBI]

DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSD

Approximately 43 kDa

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  Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm solution of 20 mM Tris-HC1, 0.5 M NaCl, 6% Trehalose, pH 8.0l or 50 mM Tris-HCL, 300 mM NaCL, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.