Skip to Content
Merck
CN

A6535

Apyrase from potatoes

ATPase ≥200 units/mg protein, lyophilized powder

Synonym(s):

Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-569-8
MDL number:
EC Number:
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

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

Looking for similar products? Visit Product Comparison Guide

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.

Physical form

Partially purified, lyophilized powder containing potassium succinate buffer salts.

Preparation Note

Derived from red potato

Other Notes

One unit will liberate 1.0 μmole of inorganic phosphate from ATP or ADP per min at pH 6.5 at 30 °C.
This grade has a low ATPase/ADPase ratio.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

低风险生物材料

This item has


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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
David Riewe et al.
Plant physiology, 147(3), 1092-1109 (2008-05-16)
Apyrases hydrolyze nucleoside triphosphates and diphosphates and are found in all eukaryotes and a few prokaryotes. Although their enzymatic properties have been well characterized, relatively little is known regarding their subcellular localization and physiological function in plants. In this study
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.

Global Trade Item Number

SKUGTIN
A6535-2KU04061833382431
A6535-100UN04061833382400
A6535-1KU04061833382417
A6535-200UN04061833382424
A6535-500UN04061833382448

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service