T4330
Turbonuclease from Serratia marcescens
recombinant, expressed in E. coli
Synonyma:
Endonuclease from Serratia marcescens
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Číslo CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Doporučené produkty
biological source
Serratia marcescens
Quality Level
recombinant
expressed in E. coli
form
liquid
concentration
≥200,000 units/mL
technique(s)
DNA purification: suitable
suitability
suitable for cell lysis
application(s)
life science and biopharma
storage temp.
−20°C
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General description
Endonuclease from Serratia marcescens is a dimer containing two identical monomeric units with distinct protein folds. The core contains a six-stranded antiparallel β-sheet flanked by α-helices on either side. Each monomer bears one active site. This enzyme is a magnesium-dependent nucleases.
Application
Turbonuclease from Serratia marcescens has been used for cell lysis during proximity biotinylation assay (BioID) and affinity-purification. It has also been used as a component of lysis buffer for protein extraction from cell lines for affinity purification studies.
Turbonuclease has been used in a study to assess the TY3 gag3 spacer effect on intracellular condensation and uncoating.
Used for the removal of nucleic acid from protein samples.
Biochem/physiol Actions
Endonuclease from Serratia marcescens is effective against both single- and double-stranded DNA and RNA. It mediates the digestion of the 3′ O—P bond resulting in oligonucleotides ending with 5′ monophosphate. The activity of this enzyme is known to be less affected by the reducing and chaotropic agents. It is highly stable at room temperature. This endonuclease eliminates the undesired nucleic acids in downstream processing.
Turbonuclease provides a nuclease treatment by reducing viscosity and degrading RNA, genomic DNA, baculovirus DNA, and unencapsidated vector DNA.
Digests native or heat-denatured DNA and RNA.
Unit Definition
One unit will digest sonicated salmon sperm DNA to acid-soluble oligonucleotides equivalent to a ΔA260 of 1.0 in 30 min at pH 8.0 at 37 °C.
Physical form
Supplied as a solution in 50 mM Tris-HCl, pH 8.0 and 50 mM NaCl
Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Zákazníci si také prohlíželi
M D Miller et al.
Journal of molecular biology, 288(5), 975-987 (1999-05-18)
Serratia endonuclease is an important member of a class of magnesium dependent nucleases that are widely distributed in nature. Here, we describe the location and geometry of a magnesium-water cluster within the active site of this enzyme. The sole protein
Kristina Clemens et al.
Journal of virology, 85(7), 3055-3066 (2011-01-29)
Cells expressing the yeast retrotransposon Ty3 form concentrated foci of Ty3 proteins and RNA within which virus-like particle (VLP) assembly occurs. Gag3, the major structural protein of the Ty3 retrotransposon, is composed of capsid (CA), spacer (SP), and nucleocapsid (NC)
Sylvain Cecchini et al.
Human gene therapy, 22(8), 1021-1030 (2011-03-09)
The large amounts of recombinant adeno-associated virus (rAAV) vector needed for clinical trials and eventual commercialization require robust, economical, reproducible, and scalable production processes compatible with current good manufacturing practice. rAAV produced using baculovirus and insect cells satisfies these conditions;
Madhuri Gade et al.
JACS Au, 1(12), 2349-2360 (2022-01-04)
Protein conformational changes can facilitate the binding of noncognate substrates and underlying promiscuous activities. However, the contribution of substrate conformational dynamics to this process is comparatively poorly understood. Here, we analyze human (hMAT2A) and Escherichia coli (eMAT) methionine adenosyltransferases that
Marion Schuller et al.
Science advances, 7(16) (2021-04-16)
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) macrodomain within the nonstructural protein 3 counteracts host-mediated antiviral adenosine diphosphate-ribosylation signaling. This enzyme is a promising antiviral target because catalytic mutations render viruses nonpathogenic. Here, we report a massive crystallographic screening
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