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Acid Phosphatase

grade II, from potato

phosphatase, acid
Número da licença da enzima:

Nível de qualidade




specific activity

~2 units/mg protein (at 25 °C with 4-nitrophenyl phosphate as the substrate)


pkg of 500 mg



pH ideal


enviado em

wet ice

Categorias relacionadas

Descrição geral

Orthophosphoric-monoester phosphohydrolase (acid optimum).
Acid phosphatase is a non-specific phosphomonoesterase, found in the cytoplasmic and cell wall sections of swelling potato tubers. It possesses several acidic amino acid residues. It is found to be present in up to six isoforms with varying degree of glycosylation. The major potato isoform is a homodimer having a molar mass of 96kDa.

Ações bioquímicas/fisiológicas

Acid phosphatase maintains the concentration of inorganic phosphate. It hydrolyzes orthophosphate monoesters under acidic conditions and also takes part in tuber development in potatoes. It eliminates phosphate groups from phosphoproteins, such as casein, riboflavin binding protein, pepsinogen, ovalbumin, and phosvitin.

Armazenamento e estabilidade

Store at 2 to 8 °C. (Store dry!)

Outras notas

For life science research only. Not for use in diagnostic procedures.

Código de classe de armazenamento

11 - Combustible Solids



Ponto de fulgor (ºF)

does not flash

Ponto de fulgor (ºC)

does not flash

Certificado de análise

Certificado de origem

Acid phosphatases
H Bull
Journal of Clinical Pathology, 55, 65-72 (2002)
Da-Yong Wang et al.
Journal of integrative plant biology, 50(6), 733-741 (2008-08-21)
APase activity is involved in regulating many physiological and developmental events by affecting the resorption process. In this study, we investigate the role of APase activity in tuber development in potato. APase activities were mainly localized in cytoplasm, gaps among
K. S. Gellatly et al.
Plant physiology, 106(1), 223-232 (1994-09-01)
The major acid phosphatase (APase) from potato (Solanum tuberosom L. cv Chiefton) tubers has been purified 2289-fold to near homogeneity and a final O-phospho-L-tyrosine (P-Tyr) hydrolyzing specific activity of 1917 [mu]mol Pi produced min-1 mg-1 of protein. Nondenaturing polyacrylamide gel
Sanaullah Khan et al.
Natural product research, 30(5), 570-573 (2015-04-19)
Acid phosphatase-I (Apase-I) from seeds of Nelumbo nucifera was purified to electrophoretic homogeneity by combination of ammonium sulfate precipitation, size-exclusion and ion exchange chromatography. SDS-PAGE of purified Apase-I gave a single band with molecular mass of 80 kDa under reducing
E W Bingham et al.
Biochimica et biophysica acta, 429(2), 448-460 (1976-04-08)
Potato acid phosphatase (EC was used to remove the eight phosphate groups from alphas1-casein. Unlike most acid phosphatases, which are active at pH 6.0 or below, potato acid phosphatase can catalyze the dephosphorylation of alphas1-casein at pH 7.0. Although

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