N9914
Polynucleotide phosphorylase from Synechocystis sp.
recombinant, expressed in E. coli
Sinonimo/i:
PNPase, Polyribonucleotide Nucleotidyltransferase
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About This Item
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54
Prodotti consigliati
Origine biologica
bacterial (Synechocystis sp.)
Livello qualitativo
Ricombinante
expressed in E. coli
Descrizione
Histidine tagged
Saggio
90% (SDS-PAGE)
Forma fisica
solution
Attività specifica
≥500 units/mg protein
PM
85 kDa
tecniche
cell based assay: suitable
Compatibilità
suitable for molecular biology
applicazioni
cell analysis
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
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Descrizione generale
Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase.
Applicazioni
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.
Azioni biochim/fisiol
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.
Definizione di unità
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
Codice della classe di stoccaggio
12 - Non Combustible Liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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Patricia Bralley et al.
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
Ruth Rott et al.
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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