N9914
Polynucleotide phosphorylase from Synechocystis sp.
recombinant, expressed in E. coli
Synonym(s):
PNPase, Polyribonucleotide Nucleotidyltransferase
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
bacterial (Synechocystis sp.)
Quality Level
recombinant
expressed in E. coli
description
Histidine tagged
assay
90% (SDS-PAGE)
form
solution
specific activity
≥500 units/mg protein
mol wt
85 kDa
technique(s)
cell based assay: suitable
suitability
suitable for molecular biology
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Looking for similar products? Visit Product Comparison Guide
General description
Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase.
Application
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 Actions
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.
Unit Definition
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
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
Steven W Hardwick et al.
Open biology, 2(4), 120028-120028 (2012-06-23)
Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3'-5' directionality and processive behaviour. Its ring-like, trimeric architecture creates a central channel where phosphorolytic active sites reside. One face of the ring is decorated with RNA-binding K-homology
Elinne Becket et al.
Journal of bacteriology, 194(20), 5613-5620 (2012-08-21)
Polynucleotide phosphorylase (PNP) plays a central role in RNA degradation, generating a pool of ribonucleoside diphosphates (rNDPs) that can be converted to deoxyribonucleoside diphosphates (dNDPs) by ribonucleotide reductase. We report here that spontaneous mutations resulting from replication errors, which are
Yulia Redko et al.
Nucleic acids research, 41(1), 288-301 (2012-10-25)
Protein complexes directing messenger RNA (mRNA) degradation are present in all kingdoms of life. In Escherichia coli, mRNA degradation is performed by an RNA degradosome organized by the major ribonuclease RNase E. In bacteria lacking RNase E, the existence of
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service