Lectin XN-IL
Xenorhabdus nematophila lectin specific to hyaluronan and low/medium-sulfated heparan sulfate.
Prices
| Product number | Product | Form | Package size | In stock | Lot number | Price |
|---|---|---|---|---|---|---|
| GL-011 | XN-IL lectin | lyophilized | 1 mg | - | - | - |
| 5 mg | - | - | - | |||
| 5x 1 mg | - | - | - | |||
| 10 mg | - | - | - | |||
| bulk orders | ||||||
| Discounts may be applied for bulk orders. Biotinylated or fluorescently labeled (DyLight) variants can be provided upon request. Contact us at contact@4glyco.cz for prices and availability of those products. | ||||||
| Product Specification Sheet | .pdf 163 kB |
|---|---|
| Certificate Of Analysis (Lot Number XXXXXX) | . 0 B |
This product is for R&D use only. Not for human or animal use.
Basic information:
| Name: | XN-IL |
| Organism: | Xenorhabdus nematophila |
| Expression host: | Escherichia coli |
| Tags: | no |
| Molar mass (monomer): | 13692.6 Da |
| Extinction coefficient: | 26930 M-1 cm-1 |
| Oligomeric state: | tetramer |
| PDB code: | 9T91 (with HA tetrasaccharide) |
Protein sequence:
MYDWSGTVPAKLEQGQPTGLILKAGDVISIVAKGWVKYGYPDNYWAAPQGTLPKKPTLNDTLIAKIGNKTYGIGNGVLHKTVPVDGELILLFNDKPGSFGDNSGEFHVVIKIESRYDPDYLEEII
Carbohydrate specificity:
XN-IL binds hyaluronan and low- to medium-sulfated heparan sulfate ligands. In solution, the interaction leads to the precipitation of these GAGs. The binding occurs over a broad pH range (4-9) and is not significantly affected by the ionic strength of the buffer. The interaction is reversible, and the addition of EDTA disrupts the XN-IL/GAG complex. In contrast, XN-IL shows negligible binding to monosaccharides; lactose (disaccharide) is bound only weakly. XN-IL does not bind other glycosaminoglycans (chondroitin sulfate, high-sulfated heparan sulfate, heparin, keratan sulfate, dermatan sulfate) [1].
Stability:
The protein exhibits high thermal stability across a variety of buffers (pH range 4-10, sodium chloride concentration up to 1 M). As calcium ions in the binding sites are required for lectin activity, the addition of 0.1-0.5 mM CaCl2 to the working buffer is recommended. EDTA and other chelating agents should be avoided as they remove Ca2+ ion from the binding site and result in loss of lectin activity. After reconstitution in neutral pH buffers, the protein remains stable at 4 °C for weeks. The addition of sodium azide (0.02%) is recommended to prevent microbial growth.
Tm = 90 °C (nanoDSF, 0.1 M Hepes, pH 7.0)
Applications and biological effects:
XN-IL can be used in various applications, including lectin blotting, fluorescence microscopy, flow cytometry, and lectin histochemistry.
References:
- Korsák et al, Carbohydr Polym, 2026, doi: 10.1016/j.carbpol.2026.125557