产品名称
马铃薯来源腺苷三磷酸双磷酶, 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
在存在二价阳离子的情况下,磷酸酯酶可水解三磷酸和二磷酸核苷的磷酸酐键。它对核苷酸具有广泛的底物特异性。这种酶的这一特性使其适于许多不同的生物技术应用,包括 DNA 测序和血小板聚集抑制。
General description
腺苷三磷酸双磷酶又称 ATP-二磷酸水解酶,在各种动植物组织中都有表达。商业化的腺苷三磷酸双磷酸酶分离自马铃薯块茎。
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Subin Mao et al.
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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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