||Recombinant red fluorescence Protein (RFP)-rProtein A are produced in E. coli, and purified using multiple chromatographic steps (not affinity purified with human IgG). RFP-rProtein A bind to most mammalian immunoglobulins in their Fc binding domains and thereforeare ideal for immunofluorescence staining. The genetically engineered protein was expressed and purified from transformed E. coli containing only the IgG binding regions and have 6X His-tag on their N-terminus. Other domains such as cell wall binding region, albumin binding region and other non-specific binding regions have been eliminated from all these proteins to ensure the maximum specific IgG binding and maximal fluorescence.
||Liquid. The product is 1 mg/ml in 10 mM Phosphate buffered saline, pH 7.4 containing, 10% glycerol and 0.1% sodium azide as preservative.
||IgG Binding: >95%. Under optimal conditions, 1 mg RFP-rProtein A will bind approximately 5 mg IgG. Optimal binding of EGFP-rProtein A to antibodies occurs at pH 5.0 to 8.0 and can be eluted over a pH range of 2.5 to 3.0.
||>98% by SDS-PAGE and HPLC
||The protein is suitable as control reagent for RFP expression studies or as labeling reagent. Applications include: Flow cytometers, fluorescence microscopy, and microinjection, antibody purification, etc. at 1:100 dilution. Maximum absorption wavelength at 557 nm and emission wavelength at 585 nm.
||Store at -20 centigrade. -80 centigrade for long-term storage. Avoid exposure to light. Avoid repeated freezing and thawing.