Protein A (Sepharose) Staphylococcus aureus Protein

Specifications

Product Data
Species	Staphylococcus aureus
Concentration	lot specific
Conjugation	Sepharose
Buffer	State: Suspension of Sepharose beads (~2.0 cc suspension per cc settled beads). Buffer System: 20% (v/v) Ethanol Label: Sepharose (TM) Presentation Label: Sepharose
Preparation	Suspension of Sepharose beads (~2.0 cc suspension per cc settled beads).
Applications	Ideal for laboratory and process scale recovery and purification of monoclonal antibodies from dilute cell cultures. High capacity and high flow rate fractionation is applicable to both laboratory and scale-up processes. Protein A resin may also be used to pull down antibody:antigen complexes in immunoprecipitation experiments.  This product is suitable for use at 20 ul per immunoprecipitation reaction
Protein Description	Native Protein A (Staphylococcus aureus) coupled to bead by cyanogen bromide activation method.
Note	Matrix: Sepharose 4 Fast Flow, highly cross linked, 4% agarose derivative. Bead Size: 45-165 µm in size when swollen. Protein A/Sepharose: 6.0 mg Protein A per cc of drained sepharose gel. Binding Capacity: Approximately 35 mg Human IgG per cc of drained sepharose gel. Exclusion Limit (Mr): 3 x 10e7 Maximum Linear Flow Rate: < 1300 cm/hr pH Stability: Long term stability within pH range of 3 to 9. Short term stability within pH range of 2 to 10. Applications: Ideal for laboratory and process scale recovery and purification of monoclonal antibodies from dilute cell cultures. High capacity and high flow rate fractionation is applicable to both laboratory and scale-up processes.
Storage	Store vial at 2-8°C prior to opening. DO NOT FREEZE!
Stability	Shelf life: one year from despatch.
Bioactivity	Specific: ~35 mg Human IgG bound per cc of drained beads.
Reference Data

*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.