Analytical Data
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Gene name
HSP90
- Application
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Alternative Names
CDC37L1;CDC37B;HARC;Hsp90 co-chaperone Cdc37-like 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15185
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Expression Region
1-160aa
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AA Sequence
MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
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Molecular Weight
20.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
HSP90, or Heat Shock Protein 90, is a highly conserved molecular chaperone that plays a crucial role in protein folding, stability, and regulation within the cell. It is involved in the maturation and activation of various signaling proteins, including receptor tyrosine kinases and steroid hormone receptors, which are essential for normal cellular functions and responses to stress. Given its central role in numerous cellular processes, HSP90 has emerged as a significant target for cancer therapy, as many oncogenic proteins are dependent on HSP90 for their stability and functionality. Researchers have focused on generating recombinant HSP90 proteins to study its structure, function, and interactions with client proteins in more detail. Recombinant HSP90 allows for the examination of its biochemical properties, post-translational modifications, and interactions in controlled experimental settings, enabling a deeper understanding of its role in oncogenesis and cellular stress responses. Furthermore, the development of HSP90 inhibitors has opened new avenues for therapeutic intervention in cancer treatment. The ongoing study of HSP90 and its recombinant forms is thus vital for elucidating its complex biology and for identifying potential strategies to manipulate its activity in disease contexts, particularly in cancer and neurodegenerative disorders.
