Electrophoretic Mobility-Shift Assay (EMSA) Kit, with SYBR™ Green & SYPRO™ Ruby EMSA stains
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Invitrogen™

Electrophoretic Mobility-Shift Assay (EMSA) Kit, with SYBR™ Green & SYPRO™ Ruby EMSA stains

Dieses fluoreszenzbasierte EMSA-Kit (Electrophoretic Mobility Shift Assay) bietet eine schnelle, einfache und quantitative Methode zum Nachweis von Nukleinsäure und ProteinWeitere Informationen
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KatalognummerMenge
E330751 kit
Katalognummer E33075
Preis (EUR)
688,00
Each
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Menge:
1 kit
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Preis (EUR)
688,00
Each
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Dieses fluoreszenzbasierte EMSA-Kit (Electrophoretic Mobility Shift Assay) bietet eine schnelle, einfache und quantitative Methode zum Nachweis von Nukleinsäure und Protein im gleichen Gel. Dieses Kit verwendet zwei Fluoreszenzfarbstoffe für den Nachweis: SYBR™ Green EMSA Nukleinsäure-Gel-Färbemittel für den Nachweis von RNA und DNA und SYPRO™ Ruby EMSA-Proteingel-Farbstoff für den Proteinnachweis. Die Nukleinsäuren und Proteine werden nach der Elektrophorese sequentiell im Gel gefärbt, so dass keine Möglichkeit besteht, dass die Markierung die zu untersuchende Proteinbindung beeinträchtigt. Das Färben dauert nur etwa 20 Minuten für Nukleinsäure und die anschließende Proteinfärbung etwa 4 Stunden.
Nur für Forschungszwecke. Darf nicht für diagnostische Verfahren eingesetzt werden.
Specifications
AssayEMSA (Electrophoretic Mobility Shift Assay)
NachweisverfahrenFluoreszent
ProduktlinieSYBR™, SYPRO™
ProdukttypKit für Electrophoretic Mobility-Shift-Assay (EMSA)
Menge1 kit
VersandbedingungRaumtemperatur
Unit SizeEach
Inhalt und Lagerung
Bei -5 bis -30 °C lagern und vor Licht schützen.
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Fluoreszenzspektren

Fluorescence spectra

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Zertifikate

Chargen-Nr.Certificate TypeDateCatalog Number(s)
2998018Certificate of Analysis30. März 2025E33075
2920633Certificate of Analysis08. Jan. 2025E33075
2816136Certificate of Analysis19. März 2024E33075
2720302Certificate of Analysis16. Nov. 2023E33075
2663844Certificate of Analysis13. Sept. 2023E33075
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Häufig gestellte Fragen (FAQ)

A supershift assay is a method for positively identifying a protein:DNA interaction on an EMSA. An antibody (typically 1 µg) is added to the binding reaction. During electrophoresis, the antibody:protein:DNA complex migrates slowly, causing a “supershift” compared to the “shift” caused by a protein:DNA complex. Not all antibodies will cause a supershift. Some antibodies do not bind to proteins once they are bound to DNA. Some antibodies can prevent protein:DNA interactions but can still be used to confirm the identity of a protein that causes a shift in the absence of the antibody.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

EMSAs (also called gel shifts, band shifts, gel retardation assays, or mobility assays) have been used extensively for studying protein-DNA interactions. Because protein-DNA complexes migrate more slowly through a native polyacrylamide or agarose gel than DNA alone, individual protein-DNA complexes can be visualized as discrete bands within the gel using chemiluminescence or radioisotopic detection.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

A shift assay is a DNA-binding assay using nondenaturing PAGE. It provides a simple, rapid, and extremely sensitive method for detecting sequence-specific DNA-binding proteins. Proteins bind specifically to an end-labeled DNA fragment corresponding to the individual protein-DNA complexes. You can use the assay to test binding of purified proteins or of uncharacterized factors in crude extracts. This assay also permits quantitative determination of the affinity, abundance, association rate constants, dissociation rate constants, and binding specificity of DNA-binding proteins.

A supershift assay is a variation of the mobility shift DNA-binding assay that uses antibodies to identify proteins present in the protein-DNA complex.Addition of a specific antibody to a binding reaction can have one of several effects. If the protein recognized by the antibody is not involved in complex formation, addition of the antibody should have no effect. If the protein that forms the complex is recognized by the antibody, the antibody can either block complex formation or it can form an antibody-protein-DNA ternary complex and thereby specifically result in a further reduction in the mobility of the protein-DNA complex (a supershift). Results may be different depending upon whether the antibody is added before or after the protein binds DNA (particularly if there are epitopes on the DNA binding surface of the protein).

Find additional tips, troubleshooting help, and resources within our Nucleic Acid Purification and Analysis Support Center.

Here is the composition of the 5X Binding Buffer:

- 50 mM Tris HCl, pH 7.4
- 750 mM KCl
- 0.5 mM DTT
- 0.5 mM EDTA

Note: This buffer is optimized for lac repressor binding to lac operator. It may not be optimal for other protein-nucleic acid interactions.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Zitierungen und Referenzen (14)

Zitierungen und Referenzen
Abstract
Regulation of Mn-superoxide dismutase activity and neuroprotection by STAT3 in mice after cerebral ischemia.
Authors:Jung JE, Kim GS, Narasimhan P, Song YS, Chan PH,
Journal:J Neurosci
PubMed ID:19474327
'Cerebral ischemia and reperfusion increase superoxide anions (O(2)(*-)) in brain mitochondria. Manganese superoxide dismutase (Mn-SOD; SOD2), a primary mitochondrial antioxidant enzyme, scavenges superoxide radicals and its overexpression provides neuroprotection. However, the regulatory mechanism of Mn-SOD expression during cerebral ischemia and reperfusion is still unclear. In this study, we identified the ... More
The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif.
Authors:Ohlenschläger O, Kuhnert A, Schneider A, Haumann S, Bellstedt P, Keller H, Saluz HP, Hortschansky P, Hänel F, Grosse F, Görlach M, Pospiech H,
Journal:Nucleic Acids Res
PubMed ID:22730300
'The RecQL4 helicase is involved in the maintenance of genome integrity and DNA replication. Mutations in the human RecQL4 gene cause the Rothmund-Thomson, RAPADILINO and Baller-Gerold syndromes. Mouse models and experiments in human and Xenopus have proven the N-terminal part of RecQL4 to be vital for cell growth. We have ... More
nalD encodes a second repressor of the mexAB-oprM multidrug efflux operon of Pseudomonas aeruginosa.
Authors:Morita Y, Cao L, Gould VC, Avison MB, Poole K,
Journal:J Bacteriol
PubMed ID:17028276
The Pseudomonas aeruginosa nalD gene encodes a TetR family repressor with homology to the SmeT and TtgR repressors of the smeDEF and ttgABC multidrug efflux systems of Stenotrophomonas maltophilia and Pseudomonas putida, respectively. A sequence upstream of mexAB-oprM and overlapping a second promoter for this efflux system was very similar ... More
Functional characterization of the NfxB repressor of the mexCD-oprJ multidrug efflux operon of Pseudomonas aeruginosa.
Authors:Purssell A, Poole K,
Journal:
PubMed ID:23924707
The mexCD-oprJ multidrug efflux operon of Pseudomonas aeruginosa is regulated by the NfxB repressor. Two forms of NfxB have been reported [Shiba et al. (1995). J Bacteriol 177, 5872) although mutagenesis studies here confirm that the larger protein (199 amino acids, 22.4 kDa) is the functional repressor. NfxB binds upstream ... More
Identifying cis-regulatory changes involved in the evolution of aerobic fermentation in yeasts.
Authors:Lin Z, Wang TY, Tsai BS, Wu FT, Yu FJ, Tseng YJ, Sung HM, Li WH,
Journal:Genome Biol Evol
PubMed ID:23650209
Gene regulation change has long been recognized as an important mechanism for phenotypic evolution. We used the evolution of yeast aerobic fermentation as a model to explore how gene regulation has evolved and how this process has contributed to phenotypic evolution and adaptation. Most eukaryotes fully oxidize glucose to CO2 ... More
14 total citations

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