10108227001
Roche
Acid Phosphatase
grade II, from potato
Sinonimo/i:
phosphatase, acid
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About This Item
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Prodotti consigliati
Livello qualitativo
Stato
lyophilized
Attività specifica
~2 units/mg protein (at 25 °C with 4-nitrophenyl phosphate as the substrate)
Confezionamento
pkg of 500 mg
Produttore/marchio commerciale
Roche
pH ottimale
4.9-5.6
Condizioni di spedizione
wet ice
Categorie correlate
Descrizione generale
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.[1][2] 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.[3]
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.[1][2] 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.[3]
Azioni biochim/fisiol
Acid phosphatase maintains the concentration of inorganic phosphate. It hydrolyzes orthophosphate monoesters under acidic conditions and also takes part in tuber development in potatoes.[3][4][5] It eliminates phosphate groups from phosphoproteins, such as casein, riboflavin binding protein, pepsinogen, ovalbumin, and phosvitin.[6]
Stoccaggio e stabilità
Store at 2 to 8 °C. (Store dry!)
Altre note
For life science research only. Not for use in diagnostic procedures.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
does not flash
Punto d’infiammabilità (°C)
does not flash
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I clienti hanno visto anche
Acid phosphatases
H Bull
Journal of Clinical Pathology, 55, 65-72 (2002)
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
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
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
M Kruzel et al.
Acta biochimica Polonica, 29(3-4), 321-330 (1982-01-01)
1. Acid phosphatase (AcPase) from potato tubers was purified by tannic acid fractionation, DEAE-cellulose chromatography, filtration on Bio-Gel P-150 and affinity chromatography on Con A-Sepharose. The enzyme was purified 260-fold and was electrophoretically homogeneous; its mol. mass is about 69
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