Anti-Cleaved PARP antibody (ab4830)
- Product nameAnti-Cleaved PARP antibodySee all Cleaved PARP primary antibodies ...
- DescriptionRabbit polyclonal to Cleaved PARP
- SpecificityThis antibody specifically recognizes the 85 kDa fragment of cleaved PARP and can be used as marker for detecting apoptotic cells. Cleavage Site Specific Antibody, Unconjugated. The antiserum was produced against a chemically synthesized peptide corresponding to the N-terminus of cleavage site (214/215) of human PARP and will recognize Asp 214 and Gly 215.
- Tested applicationsICC, WB more details
- Species reactivityReacts with: Cow, Human
Synthetic peptide (Human) corresponding to N-terminus of cleavage site (214/215) of human PARP.
- Positive controlHeLa cells treated with staurosporine at 0.5 µM for 5 hours or bovine PARP cleaved by caspase 3.
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: 0.05% Sodium Azide
Constituents: 50% Glycerol, PBS, 1mg/ml BSA (IgG, protease free). pH 7.4
- Concentration information loading...
- PurityImmunogen affinity purified
- Purification notesPurified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a peptide spanning the cleavage site to remove antibody that is reactive with full length PARP. The final product is generated by affinity chromatography using a peptide corresponding to the PARP cleavage site.
- Clonality Polyclonal
- Epigenetics and Nuclear Signaling
- DNA / RNA
- DNA Damage & Repair
- DNA Damage Response
- DNA Damage Recognition
Our Abpromise guarantee covers the use of ab4830 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||WB: 1/1000. Detects a band of approximately 85 kDa (predicted molecular weight: 85 kDa).|
- FunctionInvolved 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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150.
- Sequence similaritiesContains 1 BRCT domain.
Contains 1 PARP alpha-helical domain.
Contains 1 PARP catalytic domain.
Contains 2 PARP-type zinc fingers.
modificationsPhosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR.
Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites.
S-nitrosylated, leading to inhibit transcription regulation activity.
- Cellular localizationNucleus.
- ADP-Ribosyltransferase antibodyADPRT 1 antibodyADPRT antibody
- ADPRT1 antibodyAPOPAIN antibodyCaspase 3 Preproprotein antibodyCPP32 antibodyCPP32B antibodyCysteine Protease antibodyNAD(+) ADP ribosyltransferase 1 antibodyNAD(+) ADP-ribosyltransferase 1 antibodypADPRT 1 antibodyPARP 1 antibodyPARP antibodyPARP Cleavage Protease antibodyPARP-1 antibodyPARP1 antibodyPARP1_HUMAN antibodyPoly [ADP-ribose] polymerase 1 antibodyPoly ADP Ribose Polymerase antibodyPoly ADP ribose polymerase 1 antibodyPoly ADP ribose polymerase family member 1 antibodyPoly ADP ribose synthetase 1 antibodyPoly[ADP-ribose] synthase 1 antibodyPPOL antibodySCA1 antibodySREBP Cleavage Activity 1 antibodyYAMA antibody
Anti-Cleaved PARP antibody images
Proteins from cell extracts were resolved by SDS-PAGE on a 4-20% Tris glycine gel and were transferred to PVDF membrane. Membranes were incubated with either 1
µg/mL anti-PARP (pan) antibody or anti PARP cleavage site (214/215) specific antibody at 1 µg/mL. After washing, membranes were incubated with goat F(ab’)2 antirabbit IgG alkaline phosphatase and bands were detected using the Tropix WesternStar detection method. The data show that the anti-PARP cleavage site specific antibody only recognizes the 85 kDa fragment of PARP in apoptotic cells (lane 3) and does not react with full length PARP (lane 1). The PARP (pan) antibody confirms that nonapoptotic cells express full length PARP of 116 kDa (lane 2) and which is cleaved when apoptosis is induced (lane 4).
HeLa cells were induced into apoptosis with staurosporine at 0.5
µM for 5 hours (panel A) and were untreated as control (panel B). The cells were fixed in cold acetone for 5 minutes. Cells were incubated with the anti PARP cleavage site specific antibody (CCSA) at 10 µg/mL. Cells were then incubated with biotinylated goat anti-rabbit Igs followed by ABC and DAB. The data show that the anti-PARP CCSA specifically recognizes PARP in apoptotic cells. Taken together with Western blot data above, these data demonstrate the specificity of the anti-PARP CCSA for cleaved PARP.
All lanes : Anti-Cleaved PARP antibody (ab4830) at 1/1000 dilution
Lane 1 : Non-induced Jurkat cells
Lane 2 : Induced Jurkat cells
Goat Anti-Rabbit HRP
developed using the ECL technique
Performed under reducing conditions.
Predicted band size : 85 kDa
Observed band size : 85 kDa
Exposure time : 5 seconds
References for Anti-Cleaved PARP antibody (ab4830)
This product has been referenced in:
- Przygodzka P et al. Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment. BMC Cell Biol 11:30 (2010). WB ; Human . Read more (PubMed: 20433722) »
- Koryllou A et al. Cell death induced by N-methyl-N-nitrosourea, a model S(N)1 methylating agent, in two lung cancer cell lines of human origin. Apoptosis 14:1121-33 (2009). WB ; Human . Read more (PubMed: 19634013) »