Analytical Data
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Gene name
PRA1
- Application
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Alternative Names
58 kDa fibrinogen-binding mannoprotein FBP1
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Species
Candida albicans
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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
P87020
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Expression Region
16-299aa
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Molecular Weight
33.4 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
PRA1 (Protein Regulator of Apoptosis 1) is a protein that plays a crucial role in cellular processes, particularly in apoptosis and immune responses. Originally identified in studies of cancer biology and immune cell regulation, PRA1 has garnered attention for its involvement in various signaling pathways that modulate cell survival and death. Its expression has been implicated in several diseases, including cancer and autoimmune disorders, making it a potential target for therapeutic intervention. Researchers have primarily focused on elucidating the molecular mechanisms by which PRA1 influences apoptosis, exploring its interactions with crucial proteins involved in cell cycle regulation and death pathways. Additionally, studies have aimed to characterize its structural features and post-translational modifications, which are essential for understanding its functional diversity. The ongoing exploration of PRA1's role in apoptosis and beyond continues to shed light on its significance in health and disease, paving the way for potential applications in biomedicine, such as cancer treatment and immunotherapy. As such, the investigation into PRA1 and its recombinant protein applications has gained momentum, promising exciting avenues for both basic research and clinical applications.
