Purification Media, Affinity, Protein A Beads

The origin of Protein A is from the bacteria Staphylococcus aureus. Protein A is capable of binding most classes and subclasses of immunoglobulins from goat, rabbit, mouse and human., Protein A beads are produced using genetically engineered form of Protein A. Nonessential regions have been removed while leaving the immunoglobulins binding sites intact. The recombinant Protein A has been immobilized to agrose beads using TargetLock chemistry, in order to create a more stable product for the affinity purification and immunoprecipitation of various mammalian immunoglobulins. Protein A beads are being routinely used for the isolation of IgG from several species of mammals. The binding of Protein A to IgGs vary between animal species and between IgG subclasses within the same species. Major limitation of protein A lies with the weak binding it presents towards mouse IgG1, a common IgG subclass. Despite that, Protein A possesses useful, properties that make it a popular choice for the isolation of most types of IgGs. Protein A binds IgGs through the Fc region of the molecules leaving the Fab region available for binding the antigen. Protein A Beads are commomnly used for antibodies purification and for the isolation of immune complexes by Immunoprecipitation. Protein A Beads Specifications: , Matrix: , Sepharose CL-4B, Coupling method: TargetLock. Protein A Density: 2-4mg/ml of resin , Binding Capacity: , ~4-8mg rabbit IgG per ml of resin, Mean bead size: 40 -165um, Bead structure: Highly cross-linked spherical agarose, 4%, Max back pressure: 0.3 MPa, 3 bar, Max. flow rate: 4 ml/min/cm2, Recommended flow rate: 1-3 ml/min/cm2, Stability of the matrix: pH 2-11, Storage and Stability: May be stored at 4°C. Do not freeze. Stable for at least 6 months.