A6237
Apyrase from potato
recombinant, expressed in Pichia pastoris, ATPase ≥1000 units/mg protein, lyophilized powder
동의어(들):
Apyrase from potato, Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase
제품 이름
Apyrase from potato, recombinant, expressed in Pichia pastoris, ATPase ≥1000 units/mg protein, lyophilized powder
recombinant
expressed in Pichia pastoris
form
lyophilized powder
ATPase activity
≥1000 units/mg protein
shipped in
wet ice
storage temp.
−20°C
Quality Level
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.
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Subin Mao et al.
Lab on a chip, 21(16), 3128-3136 (2021-06-29)
Integrins are key players in platelet adhesion and aggregation. Integrin molecular tensions, the forces transmitted by integrin molecules, are regulated by both mechanical and biochemical cues, and the outside-in and inside-out signaling has been extensively studied. While the mechanical properties
Xuan Zhang et al.
European journal of medicinal chemistry, 199, 112397-112397 (2020-05-11)
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
Celia Cordero-Sanchez et al.
Blood advances, 6(15), 4471-4484 (2022-06-14)
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
Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum).
Nourizad N, et al.
Protein Expression and Purification, 27(2), 229-237 (2003)
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)
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