recB Antibody

Code CSB-PA357378XA01ENV
Size US$299
Image
  • Western Blot
    Positive WB detected in: recombinant protein
    All lanes: recB Antibody at 1:1000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 29 kDa
    Observed band size: 29 kDa
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) recB Polyclonal antibody
Uniprot No.
Target Names
recB
Alternative Names
RecBCD enzyme subunit RecB (EC 3.1.11.5) (Exodeoxyribonuclease V 135 kDa polypeptide) (Exodeoxyribonuclease V beta chain) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB) recB ior rorA b2820 JW2788
Raised in
Rabbit
Species Reactivity
Escherichia coli (strain K12)
Immunogen
Recombinant Escherichia coli (strain K12) recB protein (210-420aa)
Immunogen Species
Escherichia coli (strain K12)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions.
Gene References into Functions
  1. Multiple ssDNA translocases within the RecBCD complex both before and after chi ensures processive unwinding of DNA substrates required for efficient recombination events. PMID: 29032606
  2. This is the first occasion that RecBCD has been demonstrated to be inhibited by DNA adducts induced by cisplatin or UV. In addition, we quantified the amounts of DNA remaining after RecBCD treatment and observed that the level of inhibition was concentration and dose dependent. A DNA-targeted 9-aminoacridinecarboxamide cisplatin analogue was also found to inhibit RecBCD activity. PMID: 29129691
  3. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. PMID: 27644322
  4. A new role of the RecBCD complex in the processing of DNA single-strand gaps that are generated at DNA replication-blocking lesions: independently of its nuclease or helicase activities, the entire RecBCD complex is required for recombinational repair of the gap and efficient translesion synthesis. PMID: 28369478
  5. Sequence-dependent nanometer-scale conformational dynamics of individual RecBCD-DNA complexes has been reported. PMID: 27220465
  6. RecBCD is required to complete chromosomal replication. (Review) PMID: 26003632
  7. A mutation within RecB (Y803H) that slows the primary translocation rate of RecBC also slows the secondary translocation rate to the same extent. PMID: 22820092
  8. Study hypothesized that RuvAB catalyzes replication fork reversal, RecJ and XonA blunt the double-strand end, and then RecBCD loads RecA4142 onto this end to produce SOS(Con) expression. PMID: 20304994
  9. crystal structure of RecBCD bound to a DNA substrate PMID: 15538360
  10. RecBCD enzyme overproduction impairs DNA repair and homologous recombination in Escherichia coli. PMID: 15808933
  11. Data suggest that RecBC and RecBCD destabilize six base pairs on binding to a blunt DNA duplex end in the absence of ATP, and that a loop can form on RecBC or RecBCD binding to DNA duplexes containing a pre-formed 3'-ssDNA tail with n > or =6 nucleotides. PMID: 16126227
  12. Together, these results strongly indicate that RecD overproduction prevents dissociation of RecBCD enzyme from DNA substrate and thus increases its processivity. PMID: 16377056
  13. The kinetics of the RecBCD-catalyzed reaction with small, single-stranded oligodeoxyribonucleotide substrates under single-turnover conditions using rapid-quench flow techniques, was studied. PMID: 16887145
  14. Data suggest models for the molecular mechanism of Gam-mediated inhibition of RecBCD, and propose that Gam could be a mimetic of single-stranded, and perhaps also double-stranded, DNA. PMID: 17544443
  15. Data show that Gam inhibits the binding of RecBCD to double-stranded DNA ends, even if RecBCD is bound to DNA before its interaction with Gam. PMID: 17583735
  16. Data show that the RecBCD enzyme switches lead motor subunits in response to chi recognition. PMID: 18022364
  17. genetic requirements for SOS induction after introduction of a double-strand break (DSB) by the I-SceI endonuclease in a RecA loading deficient recB mutant (recB1080) PMID: 18445487
  18. Results describe the influence of DNA end structure on the mechanism of initiation of DNA unwinding by the Escherichia coli RecBCD and RecBC helicases. PMID: 18656489

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Protein Families
Helicase family, UvrD subfamily
Database Links
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