Analytical Data
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Gene name
Siglec-15
- Application
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Alternative Names
CD33L3; CD33 antigen-like 3
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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
Q6ZMC9
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Expression Region
Phe20~Leu266
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Molecular Weight
60kDa
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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
Siglec-15, a member of the sialic acid-binding immunoglobulin-like lectins (Siglecs) family, has gained significant attention in immunology and cancer research due to its unique role in modulating immune responses. Discovered as a receptor predominantly expressed on myeloid cells, Siglec-15 is implicated in the regulation of macrophage function and T-cell activity. Its interaction with sialic acid, a common post-translational modification on glycoproteins, allows it to play a crucial role in immune evasion mechanisms employed by tumors. Research has highlighted that tumor cells often overexpress sialylated glycans, which can engage Siglec-15 and inhibit effector immune cell functions, leading to a suppressed immune response. Consequently, understanding the functional and structural characteristics of Siglec-15 is vital for developing therapeutic strategies aimed at enhancing anti-tumor immunity. Recent studies have focused on the potential of Siglec-15 as a target for immunotherapy, exploring its role as a checkpoint molecule. The generation of recombinant Siglec-15 proteins has provided valuable tools for investigating its biological functions, signaling pathways, and interactions with ligands. Such research endeavors not only deepen our understanding of immune regulation but also pave the way for innovative treatments in cancer therapy and other immune-related disorders.
