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Recombinant Human Siglec-8 (rhSiglec-8)
Binding Specificity

rhSiglec-8 specifically recognizes sulfated sialylated glycans, with highest affinity toward the Neu5Ac(α2–3)Gal(6S)β1–4GlcNAc motif - a well-characterized terminal structure containing α2-3-linked sialic acid and 6-O-sulfated galactose. It also shows detectable, though weaker, binding to related structures such as Neu5Ac(α2–3)Galβ1–4(6S)GlcNAc, where sulfation occurs on the 6-O position of the GlcNAc rather than the galactose.

This binding specificity makes rhSiglec-8 a valuable reagent for detecting and profiling sulfated sialylated glycans, particularly in studies of eosinophil biology, allergic inflammation, immune regulation, and tumor glycosylation, where these motifs are often upregulated or selectively expressed.

Binding Image
Binding Guarantee

Every batch of recombinant hSiglec-8 is rigorously validated using our in-house glycan array. This ensures consistent binding specificity and reliable performance.

Recombinant Human Siglec-8 (rhSiglec-8)

N/A

From: $350.00

rhSiglec-8 is a recombinant human sialic acid-binding lectin expressed in HEK293 cells to ensure proper protein folding.

  • Purity: >95% (by SDS-PAGE)
  • Source: Expressed in HEK293 cells; extracellular domain (ECD) of human Siglec-8 (Accession Number: NP_055257.2)
  • Tag: N-terminal 6×His tag or N-terminal 6×His tag with human Fc tag
  • Available Formats: His-tagged (monomeric) or His + human Fc-tagged (dimeric)*
    *His-tagged format remains monomeric; Fc-tagged format forms stable dimers.
  • Binding Activity: Validated using our Sulfated Glycan Array (Product Code: 10620)
  • Predicted Molecular Mass: ~46 kDa (His-tagged); ~76 kDa (His + Fc-tagged)
  • Structure: Monomer (His-tagged); dimer (His + Fc-tagged)
  • Formulation: Lyophilized from filtered PBS solution
  • Storage: Store at –20 °C; avoid repeated freeze–thaw cycles
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Description
Binding Activity

Description

rhSiglec-8 is a recombinant form of the human lectin Siglec-8, expressed in HEK293 cells to ensure proper protein folding. It includes the extracellular domain (ECD) of Siglec-8 (NCBI Reference Sequence: NP_055257.2) and is available in two formats: N-terminal 6XHis-tagged (monomeric) and His + human Fc-tagged (dimeric).

rhSiglec-8 selectively binds sulfated sialylated glycans, with the highest affinity toward Neu5Ac(α2–3)Gal(6S)β1–4GlcNAc. It also shows moderate binding to related structures with sulfation on the GlcNAc. This specificity makes rhSiglec-8 a powerful tool for detecting and profiling sulfated glycans involved in immune regulation, allergic inflammation, and tumor-associated glycosylation. The purity of rhSiglec-8 exceeds 95%, as verified by SDS-PAGE.

Applications

rhSiglec-8 is suitable for a wide range of glycobiology applications, including:

  • Lectin blotting for glycoprotein detection
  • Histological and cytological staining of cells and tissues
  • Flow cytometry for surface glycan analysis
  • Glycan profiling for biomarker discovery, disease characterization, or glycoengineering
  • Affinity capture or enrichment of sulfated glycoproteins

Available in His-tagged, biotinylated, or FITC-labeled formats to suit diverse experimental needs.

Reconstitution & Format

His-tagged format is supplied lyophilized. Reconstitute in purified H₂O to a concentration of 0.5 mg/mL.

Shipping & Storage

Shipped on dry ice.Upon receipt, store immediately at –20 to –70 °C.

Use a manual defrost freezer and avoid repeated freeze–thaw cycles.

Stability:

As supplied (lyophilized): Stable for 12 months at –20 to –70 °C

After reconstitution (sterile):1 month at 2 to 8 °C; 3 months at –20 to –70 °C

Binding Activity

The binding activity of rhSiglec-8 was evaluated using the ZBiotech Sulfated Glycan Array (Product Code: 10620). A concentration of 5 μg/mL of hFc-tagged rhSiglec-8 (Product Code: 11002HF) was applied to the array and incubated at room temperature for 1 hour. After washing, Cy3-labeled anti-human IgG Fc antibody (2.5 μg/mL) was added and incubated for an additional hour, followed by a final wash. The array was then scanned and analyzed for glycan-binding profiles.


For detailed glycan structure information, please visit our Sulfated Glycan Array page. (Click here)

rhSiglec-8 showed strong and selective binding to sulfated sialylated glycans, particularly those containing the Neu5Ac(α2–3)Gal(6S)β1–4GlcNAc motif. It also retained binding in the presence of fucose on GlcNAc, as found in sialyl Lewis X, indicating that fucosylation does not significantly interfere with its recognition of the sulfated epitope.

These results confirm that rhSiglec-8 is a robust and specific reagent for detecting sulfated α2–3 sialylated glycans, making it well-suited for applications in glycan profiling, immune research, and analysis of inflammation- or cancer-associated glycosylation patterns.

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