추천 제품
Quality Level
형태
lyophilized
특이 활성도
~2 units/mg protein (at 25 °C with 4-nitrophenyl phosphate as the substrate)
포장
pkg of 500 mg
제조업체/상표
Roche
최적 pH
4.9-5.6
배송 상태
wet ice
관련 카테고리
일반 설명
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.
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.
생화학적/생리학적 작용
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.
저장 및 안정성
Store at 2 to 8 °C. (Store dry!)
기타 정보
For life science research only. Not for use in diagnostic procedures.
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point (°F)
does not flash
Flash Point (°C)
does not flash
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Acid phosphatases
H Bull
Journal of Clinical Pathology, 55, 65-72 (2002)
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
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
E W Bingham et al.
Biochimica et biophysica acta, 429(2), 448-460 (1976-04-08)
Potato acid phosphatase (EC 3.1.3.2) 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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