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CAS RN: | Product Number: R0231
rLSL-N-Biotin [for Galβ(1-4)GlcNAc, poly LacNAc]
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Product code: R0231
Product name: rLSL-N-Biotin [for Galβ(1-4)GlcNAc, poly LacNAc]
Quantity: 1 ml per vial (1 mg/1 ml: Lowry method)
Product form: Biotin-immobilized recombinant LSL-N, Liquid
Buffer: Phosphate buffered saline [PBS] (-), pH7.4
Molecular Mass: >17 kDa
Preservative : None
The rLSL-N is an N-terminal domain of carbohydrate-binding protein (Lectin) derived from Laetiporus sulphureus. The rLSL-N gene product is expressed in Escherichia coli. This lectin preferably binds to [Galβ(1-4)GlcNAc, poly LacNAc] glycan epitopes.
Biotin is covalently linked to the protein surface. Resulting band shift caused by biotinylation is checked by SDS-PAGE. (Unbiotinylated band is mostly not observed.) The rLSL-N-Biotin shows significant interaction with asialo human transferrin (asialo hTF) possessing [asialo] glycan epitopes by lectin-ELISA analysis. According to the lectin-blotting analysis, the rLSL-N-Biotin specifically binds to β(1-4)Gal-terminated hTF but not to ungalactosylated (at the non-reducing terminal) glycoproteins such as hTF, agalacto hTF and bovine RNase B.
Store at -20°C to -80°C. Avoid repetitive freezing and thawing. After thawing the product, it’s recommended to store at 2-10°C with an additional preservative (e.g., 0.02-0.05% [w/v] sodium azide).
R0226 Recombinant Laetiporus sulphureus lectin N-Terminal Domain (= rLSL-N) expressed in Escherichia coli
R0236 rLSL-N-LecBeads [for Galβ(1-4)GlcNAc, poly LacNAc]
R0230 rPSL1a-Biotin [for Sia α(2-6)Gal]
R0232 rMOA-Biotin [for Galα(1-3)Gal]
R0233 rSRL-Biotin [for GlcNAcβ(1-2)Man, Galβ(1-3)GalNAc]
R0234 rGRFT-Biotin [for Manα(1-2)Man]
A2659 AOL-Biotin Conjugate
|Physical State (20 deg.C)||Liquid|
|Condition to Avoid||Heat Sensitive|
|Appearance||Colorless to Almost colorless clear liquid|
|Concentration(Lowry method)||0.9 to 1.5 mg/mL|
|Molecular weight||10 to 25 kDa|
|Suitability for use in ELISA tests||min. 1.0 (10 micro g/mL, OD450)|
- Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins
- Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars
- High-resolution structural insights on the sugar-recognition and fusion tag properties of a versatile β-trefoil lectin domain from the mushroom Laetiporus sulphureus
Safety Data Sheet (SDS)
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C of A & Other Certificates
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