Lyophilized. Partially purified. Also active as a lipase.
Theoretical MW (kDa):
Native protein partially purified from Wheat Germ to the 0.35-0.55 fraction by the method described by Singer, J. Biol. Chem., 174, 11 (1948)
>=0.15 units per mg dry weight. One Unit hydrolyzes one micromole of o-carboxyphenyl phosphate per minute at 25°C, pH 5.0.
Acid Phosphatase Assay
Store at -20°C.
Acid phosphatase is an esterase with broad activity at an optimal pH below 7.0. There are three isozymes, EI, EII, and EIII of similar molecular weight (55 kDa± 5 kDa). Their optimum pH's are 5.5, 4.5, and 4.0 respectively.