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Merck

W0393

Sigma-Aldrich

Monoclonal Anti-WRN in Maus hergestellte Antikörper

clone 195C, purified from hybridoma cell culture

Synonym(e):

Anti-RECQ3, Anti-RECQL2, Anti-RECQL3, Anti-Werner syndrome helicase, Anti-Werner syndrome protein

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

195C, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~167 kDa

Speziesreaktivität

human

Konzentration

~1 mg/mL

Methode(n)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 2-4 μg/mL using nuclear cell extract of HeLa cells

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... WRN(7486)

Allgemeine Beschreibung

Anti-WRN antibody, Mouse monoclonal, (mouse IgG1 isotype) is derived from the hybridoma 195C produced by the fusion of mouse myeloma cells (p3-NS1/Ag4-1) and splenocytes from BALB/c mice immunized with a recombinant fusion protein fragment of human WRN. Werner syndrome ATP-dependent helicase (WRN) is located on chromosome 8 and is 167 kDa. The WRN protein belongs to the RecQ helicase family of DNA helicases.

Immunogen

recombinant fusion protein fragment of human WRN (amino acids 1074-1432).

Anwendung

Anti-WRN antibody has been used in
  • enzyme linked immunosorbent assay (ELISA)
  • immunoblotting
  • immunoprecipitation
  • immunohistochemistry
  • western blotting

Biochem./physiol. Wirkung

Werner syndrome ATP-dependent helicase (WRN) protein has been demonstrated to possess three known catalytic activities: 3′-5′ helicase, exonuclease and ATPase activities. The C-terminal region of the protein contains a nuclear localization signal (NLS), thus targeting WRN protein to the nucleus, nucleolus and nucleoplasmic foci. The involvement of WRN in multiple DNA metabolic process suggests its function as a tumor suppressor. Mutations in the WRN protein results in Werner syndrome (WS). The epigenetic inactivation of WRN leads to loss of WRN-exonuclease activity, resulting in increased chromosomal instability and hypersensitivity to chemotherapeutic drugs.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Yuyao Tian et al.
Cell & bioscience, 14(1), 7-7 (2024-01-07)
Metabolic dysfunction is one of the main symptoms of Werner syndrome (WS); however, the underlying mechanisms remain unclear. Here, we report that loss of WRN accelerates adipogenesis at an early stage both in vitro (stem cells) and in vivo (zebrafish).
Class I histone deacetylase HDAC1 and WRN RECQ helicase contribute additively to protect replication forks upon hydroxyurea-induced arrest
Kehrli K, et al.
The Journal of Biological Chemistry, 291(47), 24487-24503 (2016)
Bidisha Saha et al.
Molecular genetics & genomic medicine, 1(1), 7-14 (2013-08-13)
Werner syndrome is a rare autosomal recessive disorder characterized by multiple features consistent with accelerated aging. It is caused by mutations in the WRN gene, which encodes a RecQ type helicase. To date, more than 70 disease-causing mutations have been
Piri Welcsh et al.
Methods (San Diego, Calif.), 108, 99-110 (2016-05-01)
Functional studies of the roles that DNA helicases play in human cells have benefited immensely from DNA fiber (or single molecule) technologies, which enable us to discern minute differences in behaviors of individual replication forks in genomic DNA in vivo.
Werner complex deficiency in cells disrupts the nuclear pore complex and the distribution of lamin B1
Li Zhi, et al.
Biochimica et Biophysica Acta - Molecular Cell Research, 1833(12), 3338-3345 (2013)

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