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UEA-I-FITC, 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.

Product Specifications

Background

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.

Certification

RUO

Other Statements

For research use only; not for use in diagnostic procedures. FOR IN VITRO LABORATORY USE ONLY

Label

ICT

Type

Lectins

Applications

IHC, ICC

Concentration

1 mg/ml

Buffer

10 mM phosphate, 150 mM NaCl, pH 7.6, 0.1 mM Calcium chloride and 0.05% sodium azide

Shipping Conditions

Ships overnight (domestic), International Priority Shipping

Storage Conditions

2-8 °C, in the dark

Storage Temperature

2-8 °C; In the dark

Target 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.

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