Euro
USD
British Pound
NULL
Product Description
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.
Biovision | 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.
