Helix pomatia (Snail) Lectin (HPA) - Pure

Product Description
Pure agglutinin HPA is isolated from edible snail, Helix pomatia, secreted by albumen gland that produces perivitelline fluid, composed of protein and polysaccharide complexes that coat each fertilized egg. HPA has the property to aggregate bacteria such as group C streptococci and Listeria monocytogenes, and ability to bind to the surface of herpesvirus. Purified lectin has shown to agglutinate blood group A red cells but not those of B or O. HPA binds GalNAc present on the Tn antigen, but not its galactosylated form, although the T antigen could also be recognized. This lectin has two main binding specificities GalNAc and GlucNac, and has an eluting sugar of N-acetylgalactosamine with a concentration of 0.2M.

HPA consists of six identical polypeptide subunits, each containing one intra-chain disulfide bond and a carbohydrate binding site, with molecular weight of 79,000 Da. HPA is a glycoprotein with roughly 7% carbohydrate content and presence of different glycoforms probable. Structure of HPA brings two sets of three binding sites on opposite hydrophilic and charged faces of the molecule in a construction that allows two bacteria to be bound at the same time, promoting aggregation and efficient protection of snail eggs.

HPA has been successfully used as an indicator of metastatic spread in a number of epithelial neoplasms including breast, colorectum, gastric, prostate and oesophageal cancers.

This product comes in a lyophilized powder form and is stored at -20 C.

Applications:
ELISA

References

• Sanchez, J. Biochemical and Structural Analysis of Helix pomatia Agglutinin (HPA): A Hexameric Lectin with a Novel Fold. The Amer. Soc. for Biochem. and Mol. Biol., Inc. (2006) 281:20171-20180.
• Schumacher, U. Does the lectin Helix pomatia agglutinin bind to hyaluronic acid in breast and colon cancer? Acta Histochem. (1996) 98(4):434-40.