Analytical Data
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Gene name
SIGLEC14
- Application
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Species
Human
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Source
E. coli
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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
Q08ET2
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Expression Region
Gln24~Leu137
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Molecular Weight
20kDa
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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
SIGLEC14 is a member of the sialic acid-binding immunoglobulin-like lectin (SIGLEC) family, predominantly expressed on the surface of immune cells. Its significance lies in its role in modulating immune responses, particularly in recognizing sialylated glycoconjugates on pathogens and infected cells, which can either enhance or inhibit immune cell activity. Research on SIGLEC14 has gained traction due to its potential implications in various diseases, including infections and autoimmune disorders. Notably, it has been implicated in the immune evasion mechanisms utilized by certain pathogens, as well as in the regulation of inflammation. The study of SIGLEC14 recombinant proteins is critical for understanding its structural properties, ligand binding mechanisms, and functional roles in immune modulation. Furthermore, advances in recombinant protein technology have enabled the production of functional SIGLEC14 proteins, facilitating high-throughput screening and therapeutic applications. Such studies could elucidate the therapeutic potential of targeting SIGLEC14 to enhance protective immune responses or mitigate excessive inflammation, thereby providing new avenues for vaccine development and immunotherapy strategies. Overall, SIGLEC14 research holds promise for translating basic immunological insights into clinical applications, contributing to advances in personalized medicine and the development of novel therapeutic agents.
