A triantennary N-acetylgalactosamine (Tri-GalNAcβ) ligand presenting three β-GalNAc residues on a branched scaffold, connected through a β-alanine linker equipped with a biotin tag through a hydrophilic PEG3 spacer. The biotin moiety binds with high affinity to streptavidin and neutravidin, enabling straightforward immobilization on chips, in wells, or on other streptavidin/neutravidin-coated platforms. This compound enables the construction of hepatocyte-targeted therapeutics and research tools that exploit the asialoglycoprotein receptor (ASGPR), which is highly expressed on liver hepatocytes and binds GalNAc-containing ligands with high affinity. The trivalent presentation of GalNAcβ residues engages multiple carbohydrate-recognition domains of ASGPR simultaneously, producing high-avidity binding that substantially exceeds the affinity of monovalent GalNAc ligands and closely mimics the geometry of clinically validated Tri-GalNAc targeting moieties used in approved GalNAc-siRNA therapeutics.