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Recombinant Calsepa (rCalsepa)
Binding Specificity

rCalsepa binds broadly to N-glycans, including high-mannose, complex, and hybrid types, by recognizing the conserved core trisaccharide Manβ1-4GlcNAcβ1-4GlcNAc (red framed). This specificity makes it a versatile glycan-binding reagent for detecting and profiling general N-glycosylation in biological samples.

Binding Image
Binding Guarantee

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

Recombinant Calsepa (rCalsepa)

N/A

From: $300.00

rCalsepa is a recombinant glycan-binding lectin derived from Calystegia sepium, expressed in E. coli for high purity and consistency.

  • Purity: >95% (by SDS-PAGE)
  • Source: Expressed in E. coli; full-length Calsepa (GenBank: U56820.1)
  • Tag: C-terminal 6X His tag
  • Available Formats: His-tagged, biotinylated*, or FITC-labeled*
    *Biotin and FITC conjugations are performed via primary amines
  • Binding Activity: Validated using our N-glycan Array (Product Code: 10602) and Catch-All Array (Product Code: 10616)
  • Predicted Molecular Mass: ~18 kDa (prior to labeling)
  • Formulation: Lyophilized from a 0.2 μm-filtered PBS solution or provided in PBS buffer
  • Storage: Store at –20 °C; protect FITC-labeled format from light; avoid repeated freeze-thaw cycles
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Description
Binding Activity

Description

rCalsepa is a recombinant form of the lectin Calsepa, derived from Calystegia sepium and expressed in E. coli with a C-terminal 6×His tag. It specifically recognizes the conserved N-glycan core trisaccharide, Manβ1-4GlcNAcβ1-4GlcNAc, allowing it to bind a broad spectrum of high-mannose, complex, and hybrid-type N-glycans. This broad specificity makes rCalsepa a versatile reagent for detecting and profiling N-glycosylation patterns in various biological samples. The purity of rCalsepa exceeds 95%, as confirmed by SDS-PAGE under reducing conditions. The gel shows a single, clear band between 15–25 kDa, consistent with the predicted molecular mass (~18 kDa).

Applications

rCalsepa 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 N-glycosylated proteins from complex biological mixtures (e.g., serum, cell lysates) using immobilized Calsepa

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 1.0 mg/mL.

Biotinylated and FITC-labeled formats are supplied as ready-to-use liquid solutions.

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 recombinant Calsepa (rCalsepa) was evaluated using the ZBiotech N-Glycan Array (Product Code: 10602). A concentration of 2 μg/mL biotinylated rCalsepa (Product Code: 11001B) was applied to the array and incubated at room temperature for 1 hour. After washing, streptavidin-Cy3 (0.2 μg/mL) was added for detection and incubated for an additional 1 hour, followed by a final wash step. The array was then scanned and analyzed for glycan-binding patterns.


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

The results demonstrated that rCalsepa binds broadly to a wide range of N-glycans, including high-mannose, hybrid, and complex types. This broad recognition profile (Figure below) confirms that rCalsepa is a versatile glycan-binding reagent, well-suited for profiling general N-glycosylation in biological samples.

 

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