Wheat Germ Coated Plates

Wheat germ-coated plates are microplates coated with wheat germ agglutinin (WGA), a lectin derived from Triticum vulgaris. WGA specifically binds to N-acetylglucosamine (GlcNAc) and sialic acid residues on glycoproteins and glycolipids. These plates are widely used in carbohydrate research, glycoprotein analysis, and various diagnostic and research applications.

Content and Properties of Wheat Germ-Coated Plates

• Material Composition:
  • Plates are typically made from polystyrene, coated with WGA via adsorption or covalent immobilization to ensure stability and long-term activity.
  • The coating creates a uniform, high-affinity surface for GlcNAc- and sialic acid-containing molecules.
• Binding Specificity:
  • Strong affinity for N-acetylglucosamine and sialic acid residues found in glycoproteins, glycolipids, and polysaccharides.
  • Effective for capturing glycosylated molecules with complex carbohydrate structures.
• Well Formats:
  • Available in 96-well and 384-well configurations for flexible assay throughput.
  • Flat-bottom designs ensure compatibility with most detection systems, such as plate readers.
• Surface Variants:
  • High-binding surfaces enhance glycoprotein immobilization.
  • Low-background formulations are available to reduce non-specific binding and improve sensitivity.

Applications of Wheat Germ-Coated Plates

• Glycoprotein Analysis:
  • Capture and analyze glycoproteins containing GlcNAc or sialic acid residues.
• Carbohydrate-Protein Interaction Studies:
  • Used to study interactions between glycoproteins, glycolipids, and carbohydrate-binding proteins.
• Diagnostics:
  • Detection of glycosylation changes in diseases such as cancer, inflammation, or infectious diseases.
• Enzyme-Linked Lectin Assays (ELLA):
  • Applied in lectin-based immunoassays for specific carbohydrate detection.
• Drug Discovery:
  • Screening for inhibitors of glycoprotein-carbohydrate interactions.

Wheat germ-coated plates are indispensable for glycoprotein and carbohydrate research, offering a robust platform for studying complex glycan structures and their biological interactions. Their high specificity for GlcNAc and sialic acid residues makes them a valuable tool in both academic research and clinical diagnostics.