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The antibody against PARP3 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 178-533 of human PARP3 (NP_005476.4) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IHC-P, IF/ICC, ELISA.
The antibody against PARP3 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 178-533 of human PARP3 (NP_005476.4) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IHC-P, IF/ICC, ELISA.
| Cat.No | ADA-02582A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PARP3 |
| Target Synonyms | IRT1; ARTD3; ADPRT3; ADPRTL2; ADPRTL3; PADPRT-3; PARP3 | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.02% sodium azide, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Rat liver | Application | ELISA, WB, IF/ICC, IHC-P |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 178-533 of human PARP3 (NP_005476.4). | Target Species | Human |
|---|---|---|---|
| Uniprot ID | Q9Y6F1 | Immunogen Sequence |
Uniprot Id
Q9Y6F1
Target Species
Human
Target Name
PARP3
Target Full Name
Protein mono-ADP-ribosyltransferase PARP3
Target Function
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage. Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation. Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks. Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ. Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRCC5 and XRCC6. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks. Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin.
Target Subcellular Location
Nucleus. Chromosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole.
Target Tissue Specificity
Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.
Target Research Area
Cancer
Target Synonyms
ADP-ribosyltransferase diphtheria toxin-like 3;ARTD3;DNA ADP-ribosyltransferase PARP3;IRT1;NAD+;ADPRT-3;Poly [ADP-ribose] polymerase 3;PARP-3;hPARP-3;Poly[ADP-ribose] synthase 3;pADPRT-3
Target Background
The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified.
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