Anti-WRN Antibody Biotin Conjugate (N428/12)
Our mouse WRN biotin conjugate monoclonal antibody from NeuroMab is produced in-house from clone N428/12. It detects human and rat WRN and is purified by Protein A chromatography. Works in ELISA, IHC, ICC, WB.
Human, Rat
ELISA, ICC, IHC, WB
Mouse
SKU: 75-423-BTN
Ships: 1-5 business days
Product Details
WRN
Werner syndrome ATP-dependent helicase, WRN RecQ Like Helicase or DNA Helicase, RecQ-Like Type 3 is encoded by the gene WRN and is a member of the WRN RecQ Like Helicase family. WRN acts as a DNA helicase that is involved in DNA repair, replication, recombination and maintenance of DNA stability. WRN is a multifunctional enzyme with ATP dependent helicase activity, and is the only RecQ helicase member that has 3’ to 5’ exonuclease activity. WRN is expressed within the central nervous system and brain Diseases associated with this gene include Werner Syndrome and Medulloblastoma.
Purified by Protein A chromatography
Lot dependent: provided at 0.3-0.5 mg/mL
Monoclonal
N428/12
IgG1
ELISA, ICC, IHC, WB
Mouse
WRN RECQ3 RECQL2
160 kDa
Fusion Protein Amino acids 38-236 (exonuclease domain) of human WRN (accession number Q14191) produced recombinantly in E. Coli
Human
Human, Rat
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography and conjugation of purified mAb. Purified mAbs are >90% specific antibody.
PBS with 0.09% azide
Biotin
No cross-reactivity reported
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
12 months from date of receipt
RECQ3; Werner syndrome ATP-dependent helicase; RECQL3; EC 3.6.4.12; DNA helicase; RecQ-like type 3; Exonuclease WRN; Werner syndrome; EC 3.1.-.-; RecQ helicase-like; RecQ protein-like 2
Q14191
UniProt Summary: Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity on partially duplex substrates. Also has 3'->5' exonuclease activity towards double-stranded (ds)DNA with a 5'-overhang. Has no nuclease activity towards single-stranded (ss)DNA or blunt-ended dsDNA. Helicase activity is most efficient with (d)ATP, but (d)CTP will substitute with reduced efficiency; strand displacement is enhanced by single-strand binding-protein (heterotrimeric replication protein A complex, RPA1, RPA2, RPA3). Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A. Plays a role in double-strand break repair after gamma-irradiation. Unwinds some G-quadruplex DNA (d(CGG)n tracts); unwinding seems to occur in both 5'-3' and 3'-5' direction and requires a short single-stranded tail. d(CGG)n tracts have a propensity to assemble into tetraplex structures; other G-rich substrates from a telomeric or IgG switch sequence are not unwound. Depletion leads to chromosomal breaks and genome instability.
UniProt Summary: Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity on partially duplex substrates. Also has 3'->5' exonuclease activity towards double-stranded (ds)DNA with a 5'-overhang. Has no nuclease activity towards single-stranded (ss)DNA or blunt-ended dsDNA. Helicase activity is most efficient with (d)ATP, but (d)CTP will substitute with reduced efficiency; strand displacement is enhanced by single-strand binding-protein (heterotrimeric replication protein A complex, RPA1, RPA2, RPA3). Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A. Plays a role in double-strand break repair after gamma-irradiation. Unwinds some G-quadruplex DNA (d(CGG)n tracts); unwinding seems to occur in both 5'-3' and 3'-5' direction and requires a short single-stranded tail. d(CGG)n tracts have a propensity to assemble into tetraplex structures; other G-rich substrates from a telomeric or IgG switch sequence are not unwound. Depletion leads to chromosomal breaks and genome instability.
7486
Shipped on ice packs

