Applications:

Lens culinaris agglutinin (LCA) has a molecular weight of approximately 49 kDa and is composed of four subunits - two of about 17kDa and two of 8 kDa. The isoelectric point of LCA is approximately pH 8.5. LCA recognizes sequences containing a-linked mannose residues. Like other mannose specific lectins, divalent cations such as calcium and manganese are required for sugar binding activity.

LCA has been employed to separate lymphocyte populations, as a potent T-cell mitogen, and as one of the most effective agents in preventing skin allograft rejection in model systems. LCA is also used to purify numerous glycoproteins (including immunoglobulins, histocompatibility antigens, α₂-macroglobulin, etc.) as well as to fractionate glycopeptides from a variety of glycoproteins.

Lens Culinaris Agglutinin isolated from Lens culinaris (lentil) seeds is coupled to heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2 x 10⁷ used as the solid-phase matrix to which the lectin is covalently bound. The attachment of the lectin to the solid phase is carefully controlled in order to preserve the activity of the lectin as well as to minimize conformational changes of the bound lectin.

Technical Specifications

• Ligand: Lens culinaris agglutinin (LCA)
• Matrix: 4B-CL (crosslinked agarose, 4%)
• Particle size range: 52 – 165 µm
• Exclusion limit: Approximately 2 x 10⁷
• Matrix activation: Cyanogen bromide
• Matrix attachment: Amino
• Ligand density: 2 – 4 mg LCA / ml drained gel
• Binding Capacity: 3 mg Mannosyl glycoprotein/ml drained gel
• Inhibiting/Eluting Sugar: a-Methylglucoside + a-Methylmannoside
• Carbohydrate for Elution: 0.1M α-Methyl Mannopyranoside or 0.1M D-Mannose in Buffer
• Blood Group Specificity: Not available
• Form: 50:50 Liquid Suspension, PBS (1x) pH 7.4 w/ 0.01% Thimerosal
• pH stability: 4 – 9

Additional Information

Additional Information