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A6535

Sigma-Aldrich

Apyrase from potatoes

ATPase ≥200 units/mg protein, lyophilized powder

Synonym(s):

Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Grade VII

Quality Level

form

lyophilized powder

ATPase activity

≥200 units/mg protein

secondary activity

≥50 % of base activity ADPase

composition

Protein, 25-60%

solubility

H2O: soluble 1.0 mg/mL

application(s)

diagnostic assay manufacturing

foreign activity

Acid Phosphatase ≤2% of base activity

storage temp.

−20°C

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Application

Apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. For hydrolysis of organic di and triphosphates, the optimal pH is 6, and for inorganic substrates, the optimal pH is 5.1. Apyrase, from Sigma, has been used in inhibition studies of platelet-aggregation .
At least two isoenzymes are found in different varieties of S. tuberosum: one with a high ATPase/ADPase ratio (∼10) and another with a low ratio (∼1).
Reaction: ATP → ADP+Pi → AMP+2Pi.

Biochem/physiol Actions

Apyrase is found in all eukaryotes and some prokaryotes. Apyrase, from potato, has a crucial role in regulating growth and development. Apyrase is involved in the inactivation of synaptic ATP as a neurotransmitter following nerve stimulation and in the inhibition of ADP induced platelet aggregation to prevent thrombosis . Divalent metal ions are required for activity and best activity is observed with calcium ion at 5 mM.

Packaging

Sold on the basis of ATPase units.

Other Notes

This grade has a low ATPase/ADPase ratio.

Unit Definition

One unit will liberate 1.0 μmole of inorganic phosphate from ATP or ADP per min at pH 6.5 at 30 °C.

Physical form

Partially purified, lyophilized powder containing potassium succinate buffer salts.

Preparation Note

Derived from red potato

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Serena Sirigu et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(47), E7448-E7455 (2016-11-07)
Direct inhibition of smooth muscle myosin (SMM) is a potential means to treat hypercontractile smooth muscle diseases. The selective inhibitor CK-2018571 prevents strong binding to actin and promotes muscle relaxation in vitro and in vivo. The crystal structure of the
Yiying Cai et al.
Microorganisms, 8(10) (2020-10-02)
Traditional in vitro time-kill studies (TKSs) require viable plating, which is tedious and time-consuming. We used ATP bioluminescence, with the removal of extracellular ATP (EC-ATP), as a surrogate for viable plating in TKSs against carbapenem-resistant Gram-negative bacteria (CR-GNB). Twenty-four-hour TKSs
Alexandra L Chang-Graham et al.
Science (New York, N.Y.), 370(6519) (2020-11-21)
Rotavirus causes severe diarrheal disease in children by broadly dysregulating intestinal homeostasis. However, the underlying mechanism(s) of rotavirus-induced dysregulation remains unclear. We found that rotavirus-infected cells produce paracrine signals that manifested as intercellular calcium waves (ICWs), observed in cell lines
Agnete Kirkeby et al.
Thrombosis and haemostasis, 99(4), 720-728 (2008-04-09)
The haematopoietic hormone erythropoietin (EPO) has neuroprotective properties and is currently being explored for treatment of stroke and other neurological disorders. Short-term, high-dose treatment with EPO seems to improve neurological function of stroke patients but may be associated with increased
Differentiation of platelet-aggregating effects of human tumor cell lines based on inhibition studies with apyrase, hirudin, and phospholipase.
E Bastida et al.
Cancer research, 42(11), 4348-4352 (1982-11-01)

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