Overview

Description

  • Nature
    Recombinant
  • Source
    Baculovirus
  • Amino Acid Sequence
    • Species
      Human

Specifications

Our Abpromise guarantee covers the use of ab75605 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

    ELISA

    SDS-PAGE

  • Form
    Lyophilised
  • Additional notes

    Reconstituted PARP1 will retain residual polyADP-ribosylation enzymatic activity.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. After reconstitution store at -20ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents (upon reconstitution in 100ul distilled water): 50mM Tris, 100mM Sodium chloride, 10mM Magnesium chloride, 1mM DTT, 1mM NAD , 10 µg/mL activated DNA, plus lyophilization stabilizers. pH 8.

  • Reconstitution
    To reconstitute,add 100µl distilled water and leave for 5 min. Vortex gently for 1 min, avoiding air bubbles. Spin briefly.

General Info

  • Alternative names
    • ADP ribosyltransferase
    • ADP ribosyltransferase (NAD+; poly (ADP ribose) polymerase)
    • ADP ribosyltransferase diphtheria toxin like 1
    • ADP ribosyltransferase NAD(+)
    • ADPRT
    • ADPRT 1
    • ADPRT1
    • ARTD1
    • msPARP
    • NAD(+) ADP ribosyltransferase 1
    • NAD(+) ADP-ribosyltransferase 1
    • pADPRT 1
    • pADPRT1
    • PARP
    • PARP 1
    • PARP-1
    • PARP1
    • PARP1_HUMAN
    • Poly (ADP ribose) polymerase 1
    • poly (ADP ribose) polymerase family, member 1
    • Poly [ADP-ribose] polymerase 1
    • Poly(ADP ribose) polymerase
    • poly(ADP ribose) synthetase
    • poly(ADP ribosyl)transferase
    • Poly[ADP ribose] synthetase 1
    • Poly[ADP-ribose] synthase 1
    • PPOL
    see all
  • Function
    Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150.
  • Sequence similarities
    Contains 1 BRCT domain.
    Contains 1 PARP alpha-helical domain.
    Contains 1 PARP catalytic domain.
    Contains 2 PARP-type zinc fingers.
  • Post-translational
    modifications
    Phosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR.
    Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites.
    S-nitrosylated, leading to inhibit transcription regulation activity.
  • Cellular localization
    Nucleus.
  • Information by UniProt

Images

  • Lane A: unmodified PARP1 LANE B: automodified PARP1 Lane B shows a smear of staining above MW 113kDa indicating polyADP-ribosylated PARP1 modified to various extents. A significant amount of automodified PARP1 did not enter the gel (top arrow). This image shows that most of the PARP1 will be at the top of the gel with a smear running up from 113kDa indicating PARP1 is automodified to various extents. There is little or no native PARP1 at 113kDa.

  • All lanes : Anti-PARP1 antibody at 5 µg/ml

    Lane 1 : PARP1 - unmodified
    Lane 2 : Recombinant Human PARP1 protein (ab75605)

    Lysates/proteins at 0.1 µg per lane.


    Predicted band size : 113 kDa
    Observed band size : >250 kDa (why is the actual band size different from the predicted?)

    No staining is visible in Lane 1 (unmodified PARP1). Lane 2 shows a smear above M.Wt 113 kda indication poly ribosylated PARP1 modified to various extents.

References

ab75605 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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