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A7646

Sigma-Aldrich

Apyrase from potatoes

ATPase ≥60 units/mg protein, lyophilized powder (partially purified)

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

biological source

potato

Quality Level

type

Grade III

form

lyophilized powder (partially purified)

ATPase activity

≥60 units/mg protein

mol wt

~49 kDa by gel filtration

composition

Protein, 30-60%

solubility

H2O: soluble 10 mg/mL, slightly hazy

application(s)

diagnostic assay manufacturing

foreign activity

Acid Phosphatase ≤5% 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. The enzyme has been used to assess the possibility of ATP involvement in intestinal lamina propria Th17 cell differentiation.
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. The molecular weight of the protein is found to be approximately 45 kDa.

Packaging

Sold on the basis of ATPase units

Other Notes

Mixture of high and low ratio isoenzymes.

Quality

Contains ≤ 5% acid phosphatase.

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.

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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Yen-Ta Chen et al.
Journal of tissue engineering and regenerative medicine, 13(12), 2155-2168 (2019-09-11)
This study tested the hypothesis that preactivated and disaggregated shape-changed platelet (PreD-SCP) therapy significantly protected rat kidney from ischemia-reperfusion (IR) injury. Adult-male Sprague-Dawley rats (n = 24) were equally categorized into Groups 1 (sham-operated control [SC]), 2 (SC + PreD-SCP)
Properties of Two Apyrases from Solanum tuberosum
Kettlun, A. et al.
Phytochemistry, 21(3), 551-558 (1982)
Koji Atarashi et al.
Nature, 455(7214), 808-812 (2008-08-22)
Interleukin (IL)-17-producing CD4(+) T lymphocytes (T(H)17 cells) constitute a subset of T-helper cells involved in host defence and several immune disorders. An intriguing feature of T(H)17 cells is their selective and constitutive presence in the intestinal lamina propria. Here we
Mathieu F Chevalier et al.
Blood, 121(1), 29-37 (2012-10-09)
Natural regulatory T cells (Tregs) participate in responses to various chronic infections including HIV. HIV infection is associated with a progressive CD4 lymphopenia and defective HIV-specific CD8 responses known to play a key role in the control of viral replication.
Nicholas J Roberts et al.
Plant physiology, 161(1), 556-567 (2012-11-09)
Nodulation in legumes requires the recognition of rhizobially made Nod factors. Genetic studies have revealed that the perception of Nod factors involves LysM domain receptor-like kinases, while biochemical approaches have identified LECTIN NUCLEOTIDE PHOSPHOHYDROLASE (LNP) as a Nod factor-binding protein.

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