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N9914
Polynucleotide phosphorylase from Synechocystis sp.
recombinant, expressed in E. coli
Synonim(y):
PNPase, Polyribonucleotide Nucleotidyltransferase
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| Gabaryty przesyłki | SKU | Dostępność | Cena netto |
|---|---|---|---|
| 100 μg | Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności | 1770,00 zł |
Informacje o tej pozycji
Specific activity:
≥500 units/mg protein
Assay:
90% (SDS-PAGE)
Biological source:
bacterial (Synechocystis sp.)
Recombinant:
expressed in E. coli
1770,00 zł
Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności
Pomoc techniczna
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Pozwól nam pomócbiological 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
General description
Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase. [1]
Application
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. [4]
Other Notes
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
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Ta pozycja | |||
|---|---|---|---|
| specific activity ≥500 units/mg protein | specific activity ≥10 units/mg protein | specific activity ≥2 units/mg protein | specific activity ≥70 units/mg protein |
| technique(s) cell based assay: suitable | technique(s) - | technique(s) - | technique(s) - |
| biological source bacterial (Synechocystis sp.) | biological source - | biological source - | biological source - |
| assay 90% (SDS-PAGE) | assay - | assay - | assay - |
| form solution | form lyophilized powder | form powder | form lyophilized powder |
| suitability suitable for molecular biology | suitability - | suitability - | suitability - |
Klasa składowania
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Powiązane treści
Instructions
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
A Danchin
DNA research : an international journal for rapid publication of reports on genes and genomes, 4(1), 9-18 (1997-02-28)
Genome comparison permits identification of chromosome regions conserved during evolution. Bacillus subtilis and Escherichia coli are so distant that there exists very few conserved landmarks in their genome organisation. Analysis of the conserved cmk rpsA cluster pinpointed the importance of
Numer pozycji handlu globalnego
| SKU | NUMER GTIN |
|---|---|
| N9914-100UG | 04061832924953 |