RSL from Ralstonia solanacearum linked to Biotin

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Cat Number : A14-1015

Molecular weight: 9.9 kDa (monomer)

Laboratory reagent for research and development only. Not for human or animal use.


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RSL from Ralstonia solanacearum linked to Biotin

RSL (Ralstonia solanacearum Lectin) linked to Biotin is a biotinylated lectin that binds specifically to fucose and related carbohydrates, making it a valuable tool for studying plant-pathogen interactions, carbohydrate recognition, and bacterial adhesion. Derived from Ralstonia solanacearum, a plant pathogen responsible for bacterial wilt in crops, this lectin is instrumental in understanding host invasion mechanisms.

Key Characteristics of RSL:

  • Function:
    • RSL is a fucose-binding lectin with specificity for L-fucose > L-galactose > D-arabinose > D-mannose. It plays a role in bacterial adhesion to plant cells and biofilm formation.
    • It interacts with H and Lewis antigens in glycoproteins, making it useful for studying glycan-mediated interactions in both plant and animal systems.
  • Structural Features:
    • RSL is a small monomeric lectin (~9.9 kDa) with structural similarity to fungal lectins.
    • It forms stable complexes with fucosylated glycans through conserved binding motifs.
    • The lectin’s binding properties are mediated by specific amino acid residues that determine its high affinity for fucose.
  • Biotin Conjugation:
    Biotin labeling enhances the utility of RSL by enabling:

    • Streptavidin-based detection: Ideal for ELISA assays, Western blotting, and pull-down experiments to study fucose-binding interactions.
    • Quantitative binding studies: Facilitates measurement of carbohydrate-binding kinetics using biotin-streptavidin systems.
    • Microscopy applications: Enables visualization of RSL binding to fucosylated targets when paired with streptavidin-fluorophore conjugates.

Applications in Research:

  1. Plant-Pathogen Interaction Studies:
    Tracks RSL’s binding to fucosylated glycans on plant cell surfaces, elucidating mechanisms of bacterial adhesion and colonization during infection.
  2. Biofilm Formation Analysis:
    Visualizes the role of RSL in stabilizing biofilm matrices by crosslinking extracellular polysaccharides, aiding in the study of biofilm architecture and inhibitor screening.
  3. Carbohydrate Recognition Studies:
    Investigates the specificity of RSL for various glycans, providing insights into glycan-mediated signaling pathways in host-pathogen systems.
  4. Drug Discovery:
    Screens inhibitors targeting RSL’s carbohydrate-binding domain to disrupt bacterial adhesion or biofilm formation, particularly in agricultural pathogens.

Production and Validation:

  • Recombinantly expressed in E. coli and purified via affinity chromatography.
  • Biotin labeling validated through binding assays with fucosylated ligands and functional studies confirming its carbohydrate specificity and adhesion properties.

This biotinylated lectin is a versatile tool for advancing research into Ralstonia solanacearum pathogenesis, glycan recognition mechanisms, and the development of anti-adhesion strategies for crop protection.

Meta Description:
“Explore RSL from Ralstonia solanacearum, a biotinylated lectin for studying fucose-specific interactions, plant-pathogen adhesion, and biofilm formation. Ideal for glycan recognition research and anti-infection strategies.”

Citations:

  1. https://www.rcsb.org/structure/2chh
  2. https://www.rcsb.org/structure/1UQX
  3. https://pubmed.ncbi.nlm.nih.gov/12153735/
  4. http://www.xray.cz/setkani/abst2014/pokorny.htm
  5. https://pmc.ncbi.nlm.nih.gov/articles/PMC9668655/
  6. https://pmc.ncbi.nlm.nih.gov/articles/PMC10306066/
  7. https://www.jstage.jst.go.jp/article/biochemistry1922/132/2/132_2_353/_pdf
  8. https://www.rcsb.org/structure/3zi8

 

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Size

1 MG, 10 MG, 5 MG

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