Mouse Anti-Arabidopsis PARP2 Antibody (CBMOAB-38138FYC)
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Specifications
| Host species | Mouse (Mus musculus) |
| Species Reactivity | A. thaliana (Arabidopsis thaliana) |
| Clone | MO38138FC |
| Specificity | This antibody binds to Arabidopsis PARP2. |
| Format | Liquid or Lyophilized |
| Storage | Store at 4°C: short-term (1-2weeks) Store at -20°C: long-term and future use |
| Purity | > 90% was determined by SDS-PAGE |
| Purification | Purified with Protein A or G affinity chromatography |
| Cellular Localization | Nucleus |
Application Information
| Application | WB, ELISA |
| Application Notes | ELISA: 1:1000-1:3000 Other applications are to be developed. The optimal dilution should be determined by the end user. |
Target
| Introduction | This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found. |
| Product Overview | Mouse Anti-Arabidopsis PARP2 (clone MO38138FC) Antibody (CBMOAB-38138FYC) is a mouse antibody against PARP2. It can be used for PARP2 detection in Western Blot, Enzyme-Linked Immunosorbent Assay. |
| Alternative Names | Poly(ADP-Ribose) Polymerase 2; ADP-Ribosyltransferase (NAD+; Poly(ADP-Ribose) Polymerase)-Like 2; ADP-Ribosyltransferase Diphtheria Toxin-Like 2; Poly (ADP-Ribose) Polymerase Family, Member 2; NAD(+) ADP-Ribosyltransferase 2; Poly[ADP-Ribose] Synthase 2; EC 2.4.2.30; PADPRT-2; ADPRTL2; ADPRT-2 |
| UniProt ID | Q11207 |
| Protein Refseq | The length of the protein is 637 amino acids long. The sequence is show below: MANKLKVDELRLKLAERGLSTTGVKAVLVERLEEAIAEDTKKEESKSKRKRNSSNDTYESNKLIAIGEFRGMIVKELREEAIKRGLDTTGTKKDLLERLCNDANNVSNAPVKSSNGTDEAEDDNNGFEEEKKEEKIVTATKKGAAVLDQWIPDEIKSQYHVLQRGDDVYDAILNQTNVRDNNNKFFVLQVLESDSKKTYMVYTRWGRVGVKGQSKLDGPYDSWDRAIEIFTNKFNDKTKNYWSDRKEFIPHPKSYTWLEMDYGKEENDSPVNNDIPSSSSEVKPEQSKLDTRVAKFISLICNVSMMAQHMMEIGYNANKLPLGKISKSTISKGYEVLKRISEVIDRYDRTRLEELSGEFYTVIPHDFGFKKMSQFVIDTPQKLKQKIEMVEALGEIELATKLLSVDPGLQDDPLYYHYQQLNCGLTPVGNDSEEFSMVANYMENTHAKTHSGYTVEIAQLFRASRAVEADRFQQFSSSKNRMLLWHGSRLTNWAGILSQGLRIAPPEAPVTGYMFGKGVYFADMFSKSANYCYANTGANDGVLLLCEVALGDMNELLYSDYNADNLPPGKLSTKGVGKTAPNPSEAQTLEDGVVVPLGKPVERSCSKGMLLYNEYIVYNVEQIKMRYVIQVKFNYKH. |
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| MO-AB-11020W | Mouse Anti-Chimpanzee PARP2 Antibody (MO-AB-11020W) |
WB
Figure 1 PARP2 plays a dominant role in DNA damage response after bleomycin treatment. Two-week old Arabidopsis plants were transferred to 0, 2.5, 5 or 10 μg/ml of bleomycin for 18 h. Total proteins were extracted, separated by SDS-PAGE and analyzed by immunoblotting using an anti-PAR antibody. Equivalent loading of lanes was verified using Ponceau S stain. All samples shown and both blots were processed in parallel within the same experiment. Similar results were obtained in three separate experiments.
WB
Figure 2 PARP2 plays a dominant role in response to ionizing irradiation. Two-week old Arabidopsis plants grown on MS plates were irradiated with 150 Gy of γ-radiation and then flash-frozen 20, 40 or 60 min after removal from the radiation source. Total proteins were then extracted, separated by SDS-PAGE and analyzed by immunoblotting with an anti-PAR antibody. 0 min sample not exposed to γ-radiation source. All samples shown in (A) were processed in parallel within the same experiment.