Analytical Data
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Gene name
SLURP2
- Application
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Alternative Names
Secreted LY6/PLAUR domain-containing protein 2 Secreted Ly-6/uPAR-related protein 2
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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
P0DP57
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Expression Region
23-97aa
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Molecular Weight
10 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
SLURP2, a member of the Ly6/uPAR protein family, has gained attention in recent years due to its diverse biological functions and potential implications in human health and disease. Initially discovered in the context of the skin's immune response, SLURP2 is mainly expressed in epithelial tissues, including the skin and mucosal surfaces. Research has revealed that SLURP2 plays a critical role in modulating inflammatory responses, and it has been implicated in autoimmune diseases, particularly in conditions like psoriasis, where its expression levels are altered. Additionally, SLURP2 exhibits antimicrobial properties, suggesting a function in innate immunity. Its interaction with nicotinic acetylcholine receptors has also been explored, linking it to neurobiological effects and potential therapeutic avenues in treating neurodegenerative diseases. As a result, a growing body of research focuses on characterizing its structure and function, with recombinant SLURP2 proteins being produced for detailed functional studies. This ongoing research aims to clarify SLURP2's mechanisms of action, explore its potential as a biomarker for disease, and identify possible therapeutic applications, underscoring its significance in both fundamental biology and clinical applications. Through these studies, SLURP2 is positioned as a promising candidate for future biomedical research, contributing to our understanding of immune regulation and potential treatments for related conditions.
