PARP-1 [ARTD1] (E988K Mutant) (human) (rec.) Control

AdipoGen Life Sciences

PARP-1 [ARTD1] (E998K Mutant) (human) (rec.) Control

10

Research Use Only

PARP-1 (ARTD1) is 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. PARP-1 positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. It forms a complex with EEF1A1 and TXK that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. PARP-1 (E988K mutant) is an inactive form of PARP-1 which can be used as a control compound. - Protein. Human full-length inactive mutant E998K of PARP-1 is fused to a HA-tag and a His-tag. Source: Sf21 cells. Liquid. In 50mM TRIS-HCl, pH 7.5, containing 100mM sodium chloride and 50mM imidazole, 0.2% NP-40 and 10% glycerol. Purity: >95% (SDS-PAGE). PARP-1 (ARTD1) is 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. PARP-1 positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. It forms a complex with EEF1A1 and TXK that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. PARP-1 (E998K mutant) is an inactive form of PARP-1 which can be used as a control compound.

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41116133