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W0393

Sigma-Aldrich

Anti-WRN antibody, Mouse monoclonal

clone 195C, purified from hybridoma cell culture

Synonym(s):

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

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About This Item

MDL number:
MFCD02264220
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

195C, monoclonal

form

buffered aqueous solution

mol wt

antigen ~167 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

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

isotype

IgG1

UniProt accession no.

Q14191

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... WRN(7486)

Related Categories

General description

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).

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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)
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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