Galectins are soluble lectins that perform a pattern recognition function in invertebrate immunity and specifically recognise β-galactoside residues via conserved carbohydrate recognition domains. However, their function in bivalve molluscs has received little attention. Herein, a galectin (ScGal2) in razor clam (Sinonovacula constricta) consisting of a 507 bp open reading frame encoding a protein of 168 amino acids was identified and characterised. The protein includes a carbohydrate recognition domain (CRD), and several residues involved in dimerisation were found. ScGal2 mRNAs were mainly detected in hemolymph and liver, and expression was upregulated significantly following challenge with Vibrio anguillarum. Recombinant rScGal2 protein displayed strong agglutination activity toward Gram-negative bacteria, and flow cytometry revealed that ScGal2 strongly promoted phagocytosis in hemocytes. These results suggest that ScGal2 plays an indispensable role in innate immunity in razor clam, and likely participates in immune recognition and clearance processes.