Cleaved PARP1 Antibody [K10A21] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 - 1:10000 IHC1:1000

Application
WB, IHC

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
113 kDa 27 kDa, 25 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human ovarian carcinoma; Rat colon; Human breast carcinoma tissue; Human ovarian carcinoma; HAP1 cells; PC-12 cells (Staurosporine, 1 uM, 3 h); RAW 264.7 cells; NIH/3T3 cells; HeLa cells; Jurkat cell (camptothecin treated); HeLa (Staurosporine, 1 uM, 3 h); HAP1 cell (Staurosporine, 1 uM, 3 h); NIH/3T3 (Staurosporine, 1 uM, 3 h); A549 cells (Staurosporine, 3 uM, 24 h)
Negative Control	MCF7 cells; NIH/3T3 cells; PC-12 cells; Jurkat cells

Datasheet & SDS

Biological Description

Specificity
Cleaved PARP1 Antibody [K10A21] detects endogenous levels of total Cleaved PARP1 protein.

Clone
K10A21

Synonym(s)
ADPRT, PPOL, PARP1, Poly [ADP-ribose] polymerase 1, PARP-1, DNA ADP-ribosyltransferase PARP1, NAD(+) ADP-ribosyltransferase 1, Poly[ADP-ribose] synthase 1, ARTD1, ADPRT 1

Background
Cleaved PARP1, or cPARP1, refers to the caspase-generated fragments, primarily the 89 kDa C-terminal and 24 kDa N-terminal pieces of full-length Poly(ADP-ribose) polymerase-1, a 116 kDa nuclear enzyme composed of zinc finger DNA-binding domains, an automodification domain, and a catalytic C-terminal region. During apoptosis, caspase-mediated cleavage at the DEVD site between Asp214 and Gly215 separates the DNA-binding domain from the enzymatic domain, abolishing PARP1’s DNA repair activity. This event marks the cell’s irreversible commitment to programmed cell death by inactivating base excision repair, preventing further depletion of cellular energy by PARP hyperactivation, and facilitating progression of the caspase cascade. The 89 kDa fragment also acts as a poly-ADP-ribose carrier, translocating to the cytoplasm where it can bind apoptosis-inducing factor (AIF) to trigger caspase-independent cell death (parthanatos) or further amplify apoptosis through mitochondrial outer membrane permeabilization. Elevated cPARP1 indicates therapy-induced apoptosis in cancers, such as after chemotherapy or radiotherapy, while its dysregulation is linked to neurodegenerative disorders like Alzheimer’s disease and to inflammation. As a biomarker, cPARP1 distinguishes apoptosis from necrosis, since lysosomal cathepsin-mediated cleavage generates different fragments and also guides the use of PARP inhibitors, which spare DNA repair in healthy cells while sensitizing tumor cells to treatment.

Background

Cleaved PARP1, or cPARP1, refers to the caspase-generated fragments, primarily the 89 kDa C-terminal and 24 kDa N-terminal pieces of full-length Poly(ADP-ribose) polymerase-1, a 116 kDa nuclear enzyme composed of zinc finger DNA-binding domains, an automodification domain, and a catalytic C-terminal region. During apoptosis, caspase-mediated cleavage at the DEVD site between Asp214 and Gly215 separates the DNA-binding domain from the enzymatic domain, abolishing PARP1’s DNA repair activity. This event marks the cell’s irreversible commitment to programmed cell death by inactivating base excision repair, preventing further depletion of cellular energy by PARP hyperactivation, and facilitating progression of the caspase cascade. The 89 kDa fragment also acts as a poly-ADP-ribose carrier, translocating to the cytoplasm where it can bind apoptosis-inducing factor (AIF) to trigger caspase-independent cell death (parthanatos) or further amplify apoptosis through mitochondrial outer membrane permeabilization. Elevated cPARP1 indicates therapy-induced apoptosis in cancers, such as after chemotherapy or radiotherapy, while its dysregulation is linked to neurodegenerative disorders like Alzheimer’s disease and to inflammation. As a biomarker, cPARP1 distinguishes apoptosis from necrosis, since lysosomal cathepsin-mediated cleavage generates different fragments and also guides the use of PARP inhibitors, which spare DNA repair in healthy cells while sensitizing tumor cells to treatment.

References
https://pubmed.ncbi.nlm.nih.gov/21176168/ https://pubmed.ncbi.nlm.nih.gov/33168626/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%