N1290
Polynucleotide phosphorylase human
Synonyme(s) :
Polyribonucleotide nucleotidyltransferase
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About This Item
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in E. coli
Forme
solution
enzyme activity
≥20 units/mg protein
Poids mol.
~90 kDa
Concentration
400-600 μg/mL protein
Conditions d'expédition
dry ice
Température de stockage
−70°C
Actions biochimiques/physiologiques
Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans.
Forme physique
supplied as a solution in 20 mM HEPES buffer, pH 7.9, with 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, ~130 mM KCl, and 20% (w/v) glycerol.
Code de la classe de stockage
12 - Non 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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Lukasz S Borowski et al.
Biochimica et biophysica acta, 1797(6-7), 1066-1070 (2010-02-02)
Protein complexes responsible for RNA degradation play important role in three key aspects of RNA metabolism: they control stability of physiologically functional transcripts, remove the unnecessary RNA processing intermediates and destroy aberrantly formed RNAs. In mitochondria the post-transcriptional events seem
Robert N Rainey et al.
Molecular and cellular biology, 26(22), 8488-8497 (2006-09-13)
Polynucleotide phosphorylase (PNPase) is an exoribonuclease and poly(A) polymerase postulated to function in the cytosol and mitochondrial matrix. Prior overexpression studies resulted in PNPase localization to both the cytosol and mitochondria, concurrent with cytosolic RNA degradation and pleiotropic cellular effects
Victoria Portnoy et al.
RNA (New York, N.Y.), 14(2), 297-309 (2007-12-18)
PNPase is a major exoribonuclease that plays an important role in the degradation, processing, and polyadenylation of RNA in prokaryotes and organelles. This phosphorolytic processive enzyme uses inorganic phosphate and nucleotide diphosphate for degradation and polymerization activities, respectively. Its structure
Hsiao-Wen Chen et al.
Molecular and cellular biology, 26(22), 8475-8487 (2006-09-13)
We recently identified polynucleotide phosphorylase (PNPase) as a potential binding partner for the TCL1 oncoprotein. Mammalian PNPase exhibits exoribonuclease and poly(A) polymerase activities, and PNPase overexpression inhibits cell growth, induces apoptosis, and stimulates proinflammatory cytokine production. A physiologic connection for
Stefan Engelen et al.
BMC genomics, 13, 69-69 (2012-02-16)
Bacterial genomes displaying a strong bias between the leading and the lagging strand of DNA replication encode two DNA polymerases III, DnaE and PolC, rather than a single one. Replication is a highly unsymmetrical process, and the presence of two
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