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Protein L

Protein L Agarose Resin

Regular price $689.60 USD
Sale price Regular price

THE SCIENCE, IN DETAIL

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Product overview

Protein L is an immunoglobulin-binding protein that was isolated from the bacteria Peptostreptococcus magnus and provides a convenient way to separate immunoglobulins from a variety of sources. rProtein L contains four immunoglobulin binding domains of the native protein and may be used for the purification of IgG, IgM, IgA and IgD containing kappa light chains from various species without interfering with the antigen binding site. Besides antibody, Protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs). Protein L is immobilized by means of covalent binding that avoids protein loss and allows for column re-use.

ABT offers 2 ml, 5 ml and 10 ml. For Bulk quantities click here.

Specifications
Description
Product Name: Protein L Agarose Resin Catalog Number: 4BCLPL-X Technical Details • Bead Geometry & Size: Spherical ~50 - 150 µm • Crosslinked: Yes • Agarose %: 4 % • Coupling Method: Covalent binding by reductive amination • Antimicrobial Agent: 20% Ethanol • Static Binding Capacity: ~10 mg human IgG/ ml resin • Storage Temperature: 2-8˚C
Scientific background
Protein L is an immunoglobulin-binding protein that was isolated from the bacteria Peptostreptococcus magnus and provides a convenient way to separate immunoglobulins from a variety of sources. rProtein L contains four immunoglobulin binding domains of the native protein and may be used for the purification of IgG, IgM, IgA and IgD containing kappa light chains from various species without interfering with the antigen binding site. Besides antibody, Protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs). Protein L is immobilized by means of covalent binding that avoids protein loss and allows for column re-use.
Technical documents

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