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T4330

Sigma-Aldrich

Turbonuclease from Serratia marcescens

recombinant, expressed in E. coli

Synonym(s):

Endonuclease from Serratia marcescens

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
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
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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