UEA-I-Biotin, Conjugated
The anti-H (O) hemagglutinating activity of Ulex europaeus has been used widely to confirm blood group O activity. UEA I binds to many glycoproteins and glycolipids containing α –linked fucose residue. The purified lectin appears to be a dimer of two distinct polypeptide chains associated by noncovalent forces. This lectin does not react with Lea active blood group substance. The native protein has pI=6.0-6.1 and exhibits a Molecular weight 60,000-68,000 during gel filtration on Sephadex column.
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UEA-I-Biotin, Conjugated
UEA-I-Biotin, Conjugated
The anti-H (O) hemagglutinating activity of Ulex europaeus has been used widely to confirm blood group O activity. UEA I binds to many glycoproteins and glycolipids containing α –linked fucose residue. The purified lectin appears to be a dimer of two distinct polypeptide chains associated by noncovalent forces. This lectin does not react with Lea active blood group substance. The native protein has pI=6.0-6.1 and exhibits a Molecular weight 60,000-68,000 during gel filtration on Sephadex column.
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Description
The anti-H (O) hemagglutinating activity of Ulex europaeus has been used widely to confirm blood group O activity. UEA I binds to many glycoproteins and glycolipids containing α –linked fucose residue. The purified lectin appears to be a dimer of two distinct polypeptide chains associated by noncovalent forces. This lectin does not react with Lea active blood group substance. The native protein has pI=6.0-6.1 and exhibits a Molecular weight 60,000-68,000 during gel filtration on Sephadex column.
