N9914
Polynucleotide phosphorylase from Synechocystis sp.
recombinant, expressed in E. coli
Sinônimo(s):
PNPase, Polyribonucleotide Nucleotidyltransferase
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About This Item
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
fonte biológica
bacterial (Synechocystis sp.)
Nível de qualidade
recombinante
expressed in E. coli
descrição
Histidine tagged
Ensaio
90% (SDS-PAGE)
forma
solution
atividade específica
≥500 units/mg protein
peso molecular
85 kDa
técnica(s)
cell based assay: suitable
adequação
suitable for molecular biology
aplicação(ões)
cell analysis
Condições de expedição
dry ice
temperatura de armazenamento
−70°C
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Descrição geral
Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase.
Aplicação
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.
Ações bioquímicas/fisiológicas
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.
Definição da unidade
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
Código de classe de armazenamento
12 - Non Combustible Liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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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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