PARP1-Trap Affinity Reagents

Novel Binding Protein for Poly ADP Ribose Polymerase 1

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Analyze PARP1 proteins in a tube

Poly (ADP-ribose) polymerase 1 (PARP1) is one of the most abundant proteins in the nucleus and is involved in many cellular processes such as DNA repair, transcriptional regulation, and modulation of chromatin structure. Our PARP1-Trap is a high quality PARP1-binding protein coupled to a monovalent matrix (agarose particles) for biochemical analysis of PARP1 and interacting partners. Use PARP1-Trap for very fast, very efficient, and very specific pull-down of endogenous PARP1 from cell extracts. A single-step protocol yields a much cleaner result, free from contaminants, in under 30 minutes. One can also use PARP11-Trap to co-immunoprecipitate interacting factors for identification and characterization (e.g. through mass spec).

PARP1-Traps utilize super-high affinity Camelidae antibody fragments that may be used for immuno-precipitation, immuno-purification and immuno-pull down experiments with up to 10-fold better purity and yield than that of classic mouse monoclonal antibodies. Compatible with a variety of source materials, Nanobody-Traps may be used with mammalian cells, tissues & organs, bacteria, yeast, and even plants. This reagent allows PARP1 to be used for immunoprecipitations, Co-IP, mass spectroscopy, and enzyme activity measurements.

PARP1-Trap for  immunoprecipitations

To the right, input (I), non-bound (FT), and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining and Western blotting. Unlike conventional antibodies, the PARP1-Trap is free from heavy and/or light chain contaminants and therefore yields cleaner results.


PARP1 Chromobody allows monitoring of DNA damage after microirradiation in real time in living cells. To the right, HeLa cells were subjected to confocal imaging upon laser microirradation. Time lapse analysis shows recruitment of PARP1 to DNA damage.

Camelidae single-domain antibodies are like IgGs on steroids

The family of animals known as Camelidae (camels, llamas, and alpacas) produce functional antibodies devoid of light chains, so-called "heavy chain" antibodies. These heavy chain antibodies recognize and bind their antigens via a single variable domain. When cleaved from their carboxy tail, these barrel-shaped structures (2x3 nm) are extraordinarily small, naturally-occurring, and intact antigen binding fragments (MW of 13 kDa). These fragments, called Nanobodies, are characterized by high specificity, affinities in the low nanomolar range, and dissociation constants in the sub-nanomolar range (typically 10- to 100-fold better than mouse IgGs). The compact size of Nanobodies makes them extremely stable at temperatures up to 70°C, and functional even in 2M NaCl or 0.5% SDS. These small and powerful antibody fragments can be used in a variety of unique applications. They will open up your research possibilities.

Specificity: Human PARP1.  Does NOT bind to PARP 2,3, and 9 Epitope: within DNA binding domain of PARP1


Specific Camelidae antibody linked to agarose bead
Part Numbers
XTA010, XTA020, XTA100, XTA200, XTA400, XTAK020


Uncoupled and purified Camelidae antibody
Part Numbers
Particle Size:

PARP1-Trap A

~90 µm when coupled to an agarose beads


No particle coupled
Storage Buffer:

PARP1-Trap A

20% EtOH


1x PBS; Preservative: 0.01% Sodium Azide
Storage and Stability:

PARPt1-Trap A

store at 4°C; stable for one year. Do not freeze.


store at 4°C; stable for one year. Do not freeze.