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Updated: Aug 24, 2026

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
Published on: June 29, 2016
A new polyclonal antibody that recognizes a human receptor for hyaluronan mediated motility
Hiroko Kuwabara1, Masahiko Yoneda, Masami Nagai
1Second Department of Pathology, Osaka Medical College, 2-7 Daigaku-machi, Takatsuki, Osaka 569-8686, Japan. pa2020@art.osaka-med.ac.jp
Abstract:
The receptor for hyaluronan mediated motility (RHAMM), a hyaluronan (HA) binding protein, has been shown to play an important role in the motility and invasiveness of malignant cells. We have developed a polyclonal antibody against human RHAMM. A new polyclonal antibody was raised against a mixture of C-terminal RHAMM, which is capable of binding to HA, and the central domain. The antibody showed immunoreactivity to these two peptides, and detected a 95 kDa protein. Immunohistochemically, RHAMM detected by the antibody was present in the cytoplasm and nucleus of malignant B cells. Binding of HA to RHAMM was almost completely blocked by this antibody. These findings suggest that our antibody recognizes RHAMM protein and is useful for blocking HA binding to RHAMM.

