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Wichtige Dokumente
N9914
Polynucleotide phosphorylase from Synechocystis sp.
recombinant, expressed in E. coli
Synonym(e):
PNPase, Polyribonucleotide Nucleotidyltransferase
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About This Item
Empfohlene Produkte
Biologische Quelle
bacterial (Synechocystis sp.)
Qualitätsniveau
Rekombinant
expressed in E. coli
Beschreibung
Histidine tagged
Assay
90% (SDS-PAGE)
Form
solution
Spezifische Aktivität
≥500 units/mg protein
Mol-Gew.
85 kDa
Methode(n)
cell based assay: suitable
Eignung
suitable for molecular biology
Anwendung(en)
cell analysis
Versandbedingung
dry ice
Lagertemp.
−70°C
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Allgemeine Beschreibung
Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase.
Anwendung
Polynucleotide phosphorylase has been used in a study to discover that a major function of PNPase is the synthesis of CDP. It has also been used in a study to investigate the enzyme responsible for RNA 3′-tail synthesis in S. coelicolor.
Biochem./physiol. Wirkung
Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity.
Polynucleotide phosphorylase localizes to the intermembrane space of mitochondria and has a critical function in regulating mitochondrial homeostasis in human cells.
Einheitendefinition
One unit will polymerize 1.0 μmole of ADP, releasing 1.0 μmole of inorganic phosphate in 15 minutes, at pH 9.1 at 37 °C.
Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, 60 mM KCl, 20% (w/v) Glycerol
Lagerklassenschlüssel
12 - Non Combustible Liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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Microbiology (Reading, England), 152(Pt 3), 627-636 (2006-03-04)
As in other bacteria, 3'-tails are added post-transcriptionally to Streptomyces coelicolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified. This paper reports on three candidates for
The Journal of biological chemistry, 278(18), 15771-15777 (2003-02-26)
The mechanism of RNA degradation in Escherichia coli involves endonucleolytic cleavage, polyadenylation of the cleavage product by poly(A) polymerase, and exonucleolytic degradation by the exoribonucleases, polynucleotide phosphorylase (PNPase) and RNase II. The poly(A) tails are homogenous, containing only adenosines in
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