Analytical Data
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Gene name
PTPRC/CD45RA
- Application
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Alternative Names
Leukocyte common antigen ;L-CAT200; CD45
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08575
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Expression Region
26-577aa
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Molecular Weight
62.8 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
HSP90AA1, a member of the heat shock protein 90 (HSP90) family, plays a crucial role in cellular stress responses and protein homeostasis. It is involved in the proper folding, stabilization, and activation of numerous client proteins, many of which are key regulators in signaling pathways, cell growth, and survival. Research has shown that HSP90AA1 is upregulated in various cancers, making it an attractive target for therapeutic intervention. Additionally, its chaperone activity is linked to the mechanics of neurodegenerative diseases, where misfolded proteins accumulate. The study of recombinant HSP90AA1 has enabled researchers to explore its functional mechanisms, client interactions, and potential as a drug target more effectively. The production of recombinant HSP90AA1 in expression systems allows for detailed characterization and functional assays, helping to elucidate its role in health and disease, and paving the way for the development of novel therapeutic strategies focused on modulating its activity. By understanding HSP90AA1’s chaperone function and the implications of its dysregulation, researchers aim to innovate treatments that can mitigate diseases associated with protein misfolding and enhance the efficacy of existing cancer therapies.
