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P4978

Sigma-Aldrich

Phosphatase, Alkaline from calf intestine

buffered aqueous glycerol solution

Synonyme(s) :

CIAP, CIP, Orthophosphoric-monoester phosphohydrolase (alkaline optimum)

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
42010105
Nomenclature NACRES :
NA.53

Qualité

for molecular biology

Forme

buffered aqueous glycerol solution

Poids mol.

~80 kDa

Concentration

≥10,000 units/mL

Numéro d'accès UniProt

Activité étrangère

DNase, RNase, none detected

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

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Description générale

Alkaline phosphatase is a phosphomonoesterase that catalyzes the cleavage of terminal phosphates from nucleic acids. The free 5′-OH can be phosphorylated with polynucleotide kinase and γ32P-ATP to produce γ32P-end-labeled nucleic acids. Linearized cloning vectors can be prevented from recircularizing by dephosphorylation with alkaline phosphatase.

Application

Commonly used to remove the 5′-terminal phosphate from nucleic acids during molecular cloning reactions.

Composants

Alkaline phosphatase is provided in a solution of 10 mM Tris-HCl (pH 8.2), 50 mM KCl, 1 mM MgCl2, and 0.1 mM ZnCl2, in 50% (w/v) glycerol. 10X CIP Buffer, Product Number C3225, is included.

Définition de l'unité

One unit will hydrolyze 1 μmole of p-nitrophenyl phosphate per min at 37 °C.

Autres remarques

Alkaline phosphatase in 5 mM EDTA (pH 8) will be irreversibly heat inactivated at 75 °C for 10 minutes.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Christopher J Moore et al.
Genes & development, 35(3-4), 286-299 (2021-01-16)
RNase E is an essential, multifunctional ribonuclease encoded in E. coli by the rne gene. Structural analysis indicates that the ribonucleolytic activity of this enzyme is conferred by rne-encoded polypeptide chains that (1) dimerize to form a catalytic site at
Yusheng Zhao et al.
Genes & development, 35(11-12), 888-898 (2021-05-15)
Plants monitor many aspects of their fluctuating environments to help align their development with seasons. Molecular understanding of how noisy temperature cues are registered has emerged from dissection of vernalization in Arabidopsis, which involves a multiphase cold-dependent silencing of the
J Juhásová et al.
Physiological research, 60(3), 559-571 (2011-03-16)
Mesenchymal stem cells (MSCs) have been repeatedly shown to be able to repair bone defects. The aim of this study was to characterize the osteogenic differentiation of miniature pig MSCs and markers of this differentiation in vitro. Flow-cytometrically characterized MSCs
Yixing Cheng et al.
Journal of biomedical nanotechnology, 10(2), 287-298 (2014-04-18)
Scaffold architecture, surface topography, biochemical and mechanical cues have been shown to significantly improve cellular events and in vivo tissue regeneration. Specifically electrospun nanofiber matrices have gained tremendous interest due to their intrinsic structural resemblance to native tissue extracellular matrix
Jean-Paul Lallès
Nutrition reviews, 72(2), 82-94 (2014-02-11)
Important protective roles of intestinal alkaline phosphatase (IAP)--including regulation of intestinal surface pH, absorption of lipids, detoxification of free nucleotides and bacterial lipopolysaccharide, attenuation of intestinal inflammation, and possible modulation of the gut microbiota--have been reviewed recently. IAP is modulated

Protocoles

CIP is used to remove 5’-phosphate groups from DNA, RNA and both ribo and deoxy-ribonucleoside triphosphates. Detailed protocol on how to dephosphorylate DNA.

Enzymatic Assay of Alkaline Phosphatase, Diethanolamine Assay (EC 3. 1. 3. 1)

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