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A6237

Sigma-Aldrich

Apyrase from potato

recombinant, expressed in Pichia pastoris, ATPase ≥1000 units/mg protein, lyophilized powder

Synonym(s):

Apyrase from potato, Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase

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About This Item

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

recombinant

expressed in Pichia pastoris

Quality Level

form

lyophilized powder

ATPase activity

≥1000 units/mg protein

shipped in

wet ice

storage temp.

−20°C

General description

Apyrase, also known as ATP-diphosphohydrolase, is expressed in wide variety of plant and animal tissues. The commercially accessible apyrase enzyme is isolated from potato tubers.

Biochem/physiol Actions

Apyrase hydrolyses the phosphoanhydride bonds of nucleoside tri- and di-phosphates in the presence of divalent cations. It has wide substrate specificity for nucleotides. This property of the enzyme makes it suitable for different biotechnical applications, including DNA sequencing and platelet-aggregation inhibition.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Targeting BCL-XL via PROTACs is a promising strategy in reducing BCL-XL inhibition associated platelet toxicity. Recently, we reported potent BCL-XL PROTAC degraders that recruit VHL or CRBN E3 ligase. However, low protein expression or mutation of the responsible E3 ligase
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Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1.
Smith T M & Kirley T L
Biochimica et Biophysica Acta, 1386(1), 65-78 (1998)
Minfei Su et al.
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Store-operated Ca2+-entry is a cellular mechanism that governs the replenishment of intracellular stores of Ca2+ upon depletion caused by the opening of intracellular Ca2+-channels. Gain-of-function mutations of the 2 key proteins of store-operated Ca2+-entry, STIM1 and ORAI1, are associated with

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