Analytical Data
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Gene name
HSP90B1
- Application
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Alternative Names
GRP94; HSPC4; TRA1
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Species
Human
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Source
E. coli
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Tag
N-His;N-StrepⅡ
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14625
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Expression Region
R43-K754
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Protein Length
Partial
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Molecular Weight
85.5 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
Related Products
Protein Description
HSP90B1, also known as heat shock protein 90 beta, is a key molecular chaperone that plays a crucial role in protein folding, stability, and maturation within the cell. This protein is particularly important in the endoplasmic reticulum (ER), where it assists in the proper folding of glycoproteins and maintains cellular homeostasis under stress conditions. Over the years, research has shown that dysregulation of HSP90B1 is associated with various diseases, including cancer and neurodegenerative disorders, making it a significant target for therapeutic interventions. The recombinant expression of HSP90B1 allows for the study of its structural properties, functional mechanisms, and interactions with other proteins. Such studies are essential for understanding its role in disease pathways and developing potential drugs that can modulate its activity. Additionally, recombinant HSP90B1 can be utilized in biotechnological applications, including vaccine development and the production of therapeutic proteins. This highlights the importance of characterizing HSP90B1 to unravel its multifaceted biological roles and its potential implications in health and disease. Researchers are focused on optimizing expression systems and purification methods to obtain functional HSP90B1, which will facilitate further studies into its chaperone activity and its effects on protein aggregation and misfolding. Ultimately, a deeper understanding of HSP90B1 could lead to novel strategies for disease treatment and prevention, capitalizing on its pivotal role in cellular protein homeostasis.
