Analytical Data
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Gene name
SIGLEC8
- Application
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Alternative Names
SAF2; SIGLEC-8; SIGLEC8L; Sialoadhesin family member 2
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NYZ4
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Expression Region
Gly70~Ser336
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Molecular Weight
59kDa
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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
Siglec-8 is a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family, predominantly expressed on eosinophils and mast cells. It plays a significant role in the regulation of immune responses, particularly in allergic reactions and asthma. The research into recombinant Siglec-8 proteins has gained momentum due to its potential therapeutic implications. Understanding its interactions with sialic acids can inform strategies to modulate eosinophil activity, making it a target for drug development in conditions characterized by eosinophilia. Studies have shown that Siglec-8 can induce apoptosis in eosinophils upon ligand binding, thus offering a mechanism to control excessive eosinophil accumulation in allergic diseases. The recombinant version of this protein allows for detailed structural and functional analyses, contributing to our understanding of its biological significance and potential as a therapeutic agent. Furthermore, the ability to produce Siglec-8 in a controlled environment opens avenues for exploring its role in both basic and applied immunology. Overall, research into recombinant Siglec-8 is important for developing innovative treatments for allergic diseases and enhancing our understanding of immune regulation.
