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P3752

Sigma-Aldrich

Phosphatase, Acid from potato

lyophilized powder, ≥0.5 unit/mg solid

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Synonym(s):
(Orthophosphoric-monoester phosphohydrolase acid optimum), Acid Phosphatase from potato
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42010102
NACRES:
NA.54

biological source

potato

form

lyophilized powder

specific activity

≥0.5 unit/mg solid

mol wt

69 kDa

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

InChI

1S/C6H10O2/c1-3-4-8-5-6(2)7/h1,6-7H,4-5H2,2H3

InChI key

GZCWLCBFPRFLKL-UHFFFAOYSA-N

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1 of 4

This Item
P1146SRE0048P1435
vibrant-m

P3752

Phosphatase, Acid from potato

vibrant-m

P1146

Phosphatase, Acid from potato

vibrant-m

SRE0048

Phosphatase, Acid from potato

vibrant-m

P1435

Phosphatase, Acid from sweet potato

biological source

potato

biological source

-

biological source

-

biological source

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

ammonium sulfate suspension

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

application(s)

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Quality Level

200

Quality Level

300

Quality Level

400

Quality Level

300

Application

Acid phosphatase is routinely used to dephosphorylate proteins and nucleic acids. Acid phosphatase is an acid hydrolase that normally resides in lysosomes. It is used as marker for the identification of lysosomes in subcellular fractionations. Acid phosphatase, product P3752, has been used as a control in order to study how Mycobacterium bovis BCG effects the levels of acid phosphatase activity in alveolar macrophages.

Biochem/physiol Actions

Acid phosphatase is a cytoplasmic lysosomal hydrolase that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate.

Unit Definition

One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 4.8 at 37 °C.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Filipe Natalio et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 23(21), 4973-4980 (2017-03-02)
Boron's unusual properties inspired major advances in chemistry. In nature, the existence and importance of boron has been fairly explored (e.g. bacterial signaling, plant development) but its role as biological catalyst was never reported. Here, we show that boric acid
I N Mbawuike et al.
Infection and immunity, 51(2), 483-489 (1986-02-01)
The kinetics of induction of the bronchoalveolar cell population (i.e., alveolar macrophages [AM], lymphocytes, and polymorphonuclear leukocytes) was studied in mice inoculated intravenously with heat-killed Mycobacterium bovis BCG. Injection of BCG at 100 and 500 micrograms but not at 10
K Zyła et al.
The British journal of nutrition, 74(1), 3-17 (1995-07-01)
An in vitro method was developed to predict inorganic P release from maize-soyabean poultry feeds containing supplemental phytase (EC 3.1.3.8), and to quantify the effect of acid phosphatase (EC 3.1.3.2), fungal protease (EC 3.4.23.6) and Aspergillus niger cellulase (EC 3.2.1.4)
Jia Zhang et al.
Biosensors & bioelectronics, 141, 111442-111442 (2019-06-30)
Phenol contains an exchangeable hydroxyl proton resonant at 4.8 ppm from the resonance frequency of water in the 1H nuclear magnetic resonance (1H NMR) spectrum, enabling itself to be detected at sub-mM concentration by either chemical exchange saturation transfer magnetic resonance
Julia R Smith et al.
Physiological genomics, 31(2), 357-363 (2007-08-09)
We have developed a method to determine the degree of phosphorylation of a peptide in a complex mixture without enrichment or operation of the mass spectrometer in negative ion mode. Yeast lysate containing known amounts of synthetic peptides (VPQLEIVPNSAEERLHSMK and

Protocols

Enzymatic Assay of Acid Phosphatase (EC 3.1.3.2)

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