PARP-1, human recombinant | 4992

Poly-ADP-ribose metabolism plays a major role in a wide range of biological processes, such as maintenance of genomic stability, transcriptional regulation, energy metabolism and apoptosis. PARP1 Enzyme, is highly purified and enzymatically active human PARP1, expressed in a baculovirus expression system. Upon addition of NAD+ and cofactors the PARP1 is automodified by the addition of ADP-ribose monomers to form poly(ADP-ribose) polymer. The PARP1 is supplied lyophilized, and upon reconstitution with water, it retains its native poly ADP-ribosylation enzymatic activity. It is useful for high-throughput enzymatic assays, visualization of the automodification reaction by SDS-PAGE and Western blotting, ELISA, standard for SDS-PAGE, and in other assays.

4992 | PARP-1 human recombinant DataSheet

Biomolecule/Target: N/A

Synonyms: Human PARP, PARP, h-PARP, rh-PARP, recombinant human PARP, PARPrecombinant PARP, PARP

Alternates names: Human PARP, PARP, h-PARP, rh-PARP, recombinant human PARP, PARPrecombinant PARP, PARP

Taglines: Involved in DNA repair and programmed cell death

NCBI Gene ID #: 4803

NCBI Gene Symbol: NGF

Gene Source: Human

Accession #: P01138

Recombinant: Yes

Source: Baculovirus

Purity by SDS-PAGEs: 95%

Assay: SDS-PAGE

Purity: N/A

Assay #2: HPLC

Endotoxin Level: N/A

Activity (Specifications/test method): N/A

Biological activity: N/A

Results: N/A

Binding Capacity: N/A

Unit Definition: N/A

Molecular Weight: 116.0 kDa

Concentration: N/A

Appearance: Lyophilized protein

Physical form description: Lyophilized solid

Reconstitution Instructions: Dissolve in 1x PBS (It is not recommended to reconstitute to a final concentration less than 100 g/ml.). This can further be diluted to other aqueous buffers.

Amino acid sequence: Recombinant human ProNGF produced in E. coli is a non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 222 amino acids with an extra N-terminal Met and having a molecular mass of 25 kDa. The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Pro-His-Ser.