A2230
Apyrase from potatoes
High Activity, ATPase ≥600 units/mg protein, lyophilized powder
Synonyme(s) :
Adénosine 5′-diphosphatase, Adénosine 5′-triphosphatase
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
potato
Forme
lyophilized powder
Qualité
High Activity
ATPase activity
≥600 units/mg protein
secondary activity
≥50 % of base activity ADPase
Composition
protein, ≥30%
Activité étrangère
Acid Phosphatase ≤2% of base activity
Conditions d'expédition
wet ice
Température de stockage
−20°C
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Application
Apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. Apyrase, from Sigma, has been used in inhibition studies of platelet-aggregation . Product A2230 is a high activity apyrase.
Au moins deux isoenzymes sont présentes dans diverses souches de S. tuberosum : l′une avec un rapport ATPase/ADPase élevé (∼ 10) et l′autre avec un rapport faible (∼ 1).
Réaction : ATP → ADP+Pi → AMP+2Pi.
Réaction : ATP → ADP+Pi → AMP+2Pi.
Actions biochimiques/physiologiques
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.
Conditionnement
Sold on the basis of ATPase units.
Définition de l'unité
One unit will liberate 1.0 μmole of inorganic phosphate from ATP or ADP per min at pH 6.5 at 30 °C.
Forme physique
Lyophilized powder containing potassium succinate buffer salts.
Notes préparatoires
Derived from red potato
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
Tsan-Yu Chiu et al.
Plant & cell physiology, 53(11), 1913-1925 (2012-10-05)
Nucleoside triphosphate diphosphohydrolases (NTPDases; apyrases) (EC 3.6.1.5) hydrolyze di- and triphosphate nucleotides, but not monophosphate nucleotides. They are categorized as E-type ATPases, have a broad divalent cation (Mg(2+), Ca(2+)) requirement for activation and are insensitive to inhibitors of F-type, P-type
Ana Carolina Ribeiro Gomes Maia et al.
Parasitology international, 62(1), 44-52 (2012-09-22)
We identified a shared B domain within nucleoside triphosphate diphosphohydrolases (NTPDases) of plants and parasites. Now, an NTPDase activity not affected by inhibitors of adenylate kinase and ATPases was detected in Leishmania infantum promastigotes. By non-denaturing gel electrophoresis of detergent-homogenized
Yong Zhang et al.
Transplant immunology, 27(4), 175-178 (2012-08-14)
To study the effects and mechanisms of the imbalance in B cell-expressed nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1)-induced ADP degradation on graft injury during acute antibody-mediated rejection (AMR). The acute AMR animal model was established in male NTPDase 1-wild-type Balb/c
Gabriane Nascimento Porcino et al.
Experimental parasitology, 132(2), 293-299 (2012-08-28)
Nucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. In this work, mouse polyclonal antibodies produced against two synthetic peptides derived
Maja Milošević et al.
Molecular and cellular biochemistry, 371(1-2), 199-208 (2012-09-08)
Extracellular nucleotides affect female reproductive functions, fertilization, and pregnancy. The aim of this study was to investigate biochemical characteristics of ATP and ADP hydrolysis and identify E-NTPDases in myometrial cell membranes from Wistar albino rats. The apparent K (m) values
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