Purification Media, Affinity, Protein G Sepharose

Protein G originated from Streptococci is a monomeric protein with a molecular weight of about 50,000kD. Protein G binds with high affinity to the Fc region of most classes and subclasses of immunoglobulins from mouse, rabbit, goat and human. Due to this binding ability, Protein G is commonly used in the purification and recovery of either polyclonal or monoclonal immunoglobulins. Recombinant Protein G used in Protein G beads is a genetically engineered form of Protein G. Non-essential regions have been removed while leaving the IgG binding sites intact. The recombinant Protein G has been immobilized on Sepharose beads in order to create a versatile product for both the purification of various mammalian immunoglobulins and for isolating immune complexes by immunoprecipitation (IP). Matrix: SepharoseTM CL-4B, Coupling Method: TargetLock , Protein G Density: 3-4mg/ml of gel, Binding Capacity: ~4-8mg rabbit IgG per ml of beads, Mean Bead Size: 40-165um, Bead Structure: Highly cross-linked spherical agarose, 4%, Max Back Pressure: 0.3MPa, 3 bar, Max. Flow Rates: 4ml/min/cm2 , Recommended Flow Rate: 1-3 ml/min/cm2, Stability of the Matrix: pH 2-11. Storage: Store gel refrigerated at 4°C in PBS pH 7.4 containing 0.1% sodium azide as a preservative, or PBS pH 7.4 containing 20% ethanol.