I understand BSA as a blocking agent and why it is commonly used, cheap and readily available. In my lab I have been mixing my protein with BSA to increase stability while running the assay. The protein in question is from a lyophilzed powder and reconstituted with water and glycerol for long term storage (-70C). When prepared in its normal buffer solution the response of the protein, immunoblotting, is weaker and less consistent than when prepared in 1% BSA to buffer solution. I have found other articles referring to BSA being used in this method as a "common industry standard," but does anyone know the mechanism by which this happens?