Analytical Data
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Gene name
SIGLEC15
- Application
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Alternative Names
SIGLEC15；CD33L3；Sialic acid-binding Ig-like lectin 15
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
20-263aa
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AA Sequence
FVRTKIDTTENLLNTEVHSSPAQRWSMQVPPEVSAEAGDAAVLPCTFTHP HRHYDGPLTAIWRAGEPYAGPQVFRCAAARGSELCQTALSLHGRFRLLGN PRRNDLSLRVERLALADDRRYFCRVEFAGDVHDRYESRHGVRLHVTAAPR IVNISVLPSPAHAFRALCTAEGEPPPALAWSGPALGNSLAAVRSPREGHG HLVTAELPALTHDGRYTCTAANSLGRSEASVYLFRFHGASGAST
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Molecular Weight
31 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
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Protein Description
Siglec-15, a member of the sialic acid-binding immunoglobulin-like lectins (Siglecs) family, is primarily expressed on various immune cells, including osteoclasts, and plays a crucial role in modulating immune responses. Recent studies have indicated that Siglec-15 may be involved in the regulation of immune tolerance and the suppression of inflammatory responses, making it a potential target for therapeutic interventions in autoimmune diseases and cancer. The unique ability of Siglec-15 to interact with sialoglycoconjugates presents significant interest in understanding its biological functions and mechanisms of action. As researchers explore the potential of Siglec-15 as a biomarker for disease progression or therapeutic response, the development of recombinant Siglec-15 proteins has become essential for in vitro studies. These recombinant proteins facilitate the investigation of Siglec-15 interactions with sialic acids and other cellular receptors, allowing for a deeper understanding of its role in immune modulation. Furthermore, studying the structural properties and signaling pathways associated with Siglec-15 can unveil new strategies for enhancing immune responses or controlling unwanted inflammation. Overall, the exploration of Siglec-15 through recombinant protein technology stands to provide valuable insights into its potential applications in immunotherapy and precision medicine.
