antibody against parp 1  (Boster Bio)

Journal: iScience

Article Title: PBX3 regulates mast cell parthanatos via TOP2A mediated DNA damage in allergic rhinitis

doi: 10.1016/j.isci.2026.115426

Figure Lengend Snippet: Regulatory role of TOP2A in mast cell apoptosis, parthanatos pathway, and inflammatory response In vitro experimental groups: CON, model, Model+OE-NC, Model+OE-TOP2A, Model+si-NC, Model+si-TOP2A. (A and B) RT-qPCR and western blot analyses were conducted to assess the mRNA and protein expression levels of TOP2A and PARP-1 in mast cells. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the CON or Model+OE-NC or Model+si-NC group. (C) TUNEL staining was performed to evaluate and visualize cell apoptosis. ∗ p < 0.05, ∗∗ p < 0.01 vs. the CON or Model+OE-NC or Model+si-NC group; scale bars, 50 μm. (D) Cell proliferation activity in each group was measured using the CCK-8 assay. ∗∗ p < 0.01 vs. the CON or Model+OE-NC or Model+si-NC group. (E and F) MMP was assessed using the JC-1 assay to evaluate mitochondrial function. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the CON or Model+OE-NC or Model+si-NC group. (G) Western blotting was used to examine the protein levels of mitochondrial AIF (Mito-AIF), cytoplasmic AIF (Cyto-AIF), and nuclear AIF (Nucleo-AIF), along with visual analysis. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the CON or Model+OE-NC or Model+si-NC group. (H and I) ELISA was employed to determine the concentrations of β-hexosaminidase, Histamine, IL-4, IL-5, and IFN-γ. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the CON or Model+OE-NC or Model+si-NC group. Data are represented as mean ± SEM ( n = 3 per group) from independent biological replicates. One-way ANOVA with Tukey’s post hoc correction for (A–D) and (F–I).

Article Snippet: Cells were then incubated overnight at 4°C with a primary antibody against PARP-1 (PB9309, BOSTER, Pleasanton, CA, USA, 1:100).

Techniques: In Vitro, Quantitative RT-PCR, Western Blot, Expressing, TUNEL Assay, Staining, Activity Assay, CCK-8 Assay, Enzyme-linked Immunosorbent Assay

Journal: iScience

Article Title: PBX3 regulates mast cell parthanatos via TOP2A mediated DNA damage in allergic rhinitis

doi: 10.1016/j.isci.2026.115426

Figure Lengend Snippet: Effects of TOP2A on DNA damage, parthanatos regulation, and degranulation in mast cells Experimental groups: Model+OE-NC, Model+OE-TOP2A, Model+si-NC, Model+si-TOP2A. (A) Western blotting was employed to determine the protein expression levels of γ-H2AX. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+si-NC group. (B and C) IF staining was performed to assess the expression of the DNA damage marker γ-H2AX in mast cells. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+si-NC group; scale bar = 50 μm. (D) Cellular senescence was evaluated using an SA-β-gal staining kit. ∗ p < 0.05, ∗∗ p < 0.01 vs. the Model+OE-NC or Model+si-NC group; scale bars, 50 μm. Experimental groups: Model+OE-NC, Model+OE-TOP2A, Model+OE-TOP2A + DOX. (E and F) RT-qPCR and western blot analyses were conducted to detect the gene and protein expression levels of TOP2A and PARP-1 under different treatment conditions. ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+OE-TOP2A group; ns, not significant ( p ≥ 0.05). (G) Western blotting was employed to determine the protein expression levels of γ-H2AX. ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+OE-TOP2A group. (H) IF staining was used to evaluate γ-H2AX expression as a marker of DNA damage. ∗ p < 0.05, ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+OE-TOP2A group; scale bars, 50 μm. (I) SA-β-gal staining was used to assess cellular senescence. ∗ p < 0.05, ∗∗ p < 0.01 vs. the Model+OE-NC or Model+OE-TOP2A group; scale bars, 50 μm. (J) Western blot analysis was used to determine the protein expression levels of Mito-AIF, Cyto-AIF, and Nucleo-AIF. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+OE-TOP2A group. (K and L) ELISA assays were carried out to measure the levels of β-hexosaminidase, Histamine, IL-4, IL-5, and IFN-γ. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+OE-NC or Model+OE-TOP2A group. Data are represented as mean ± SEM ( n = 3 per group) from independent biological replicates. one-way ANOVA with Tukey’s post hoc correction for (A and C–L).

Article Snippet: Cells were then incubated overnight at 4°C with a primary antibody against PARP-1 (PB9309, BOSTER, Pleasanton, CA, USA, 1:100).

Techniques: Western Blot, Expressing, Staining, Marker, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay

Journal: iScience

Article Title: PBX3 regulates mast cell parthanatos via TOP2A mediated DNA damage in allergic rhinitis

doi: 10.1016/j.isci.2026.115426

Figure Lengend Snippet: Effects of PBX3 silencing on mast cell function and DNA damage response Experimental groups: Model+si-NC, Model+ si-PBX3. (A) RT-qPCR and western blot analyses were conducted to evaluate the mRNA expression levels of PBX3 and TOP2A. ∗∗∗ p < 0.001 vs. the Model+si-NC group. (B–D) Western blotting and IF staining were used to assess the expression of the DNA damage marker γ-H2AX. ∗ p < 0.05, ∗∗∗ p < 0.001 vs. the Model+si-NC group; scale bars, 50 μm. (E) SA-β-gal staining was performed to detect cellular senescence. ∗∗ p < 0.01 vs. the Model+si-NC group; scale bars, 50 μm. (F–H) RT-qPCR, western blotting, and IF staining were employed to examine PARP-1 expression in mast cells. ∗∗∗ p < 0.001 vs. the Model+si-NC group; scale bars, 50 μm. (I) Western blot analysis was used to detect the protein levels of Mito-AIF, Cyto-AIF, and Nucleo-AIF. ∗∗∗ p < 0.001 vs. the Model+si-NC group. (J and K) ELISA assays were conducted to quantify the levels of β-hexosaminidase, histamine, IL-4, IL-5, and IFN-γ in mast cells. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+si-NC group. Data are represented as mean ± SEM ( n = 3 per group) from independent biological replicates. Two-tailed unpaired Student’s t tests for (A, B, D–G, and I–K).

Article Snippet: Cells were then incubated overnight at 4°C with a primary antibody against PARP-1 (PB9309, BOSTER, Pleasanton, CA, USA, 1:100).

Techniques: Cell Function Assay, Quantitative RT-PCR, Western Blot, Expressing, Staining, Marker, Enzyme-linked Immunosorbent Assay, Two Tailed Test

Journal: iScience

Article Title: PBX3 regulates mast cell parthanatos via TOP2A mediated DNA damage in allergic rhinitis

doi: 10.1016/j.isci.2026.115426

Figure Lengend Snippet: PBX3 drives DNA damage through TOP2A to regulate mast cell parthanatos, senescence, and degranulation Experimental groups: Model+si-NC, Model+si-PBX3, Model+si-PBX3+OE-NC, Model+si-PBX3+OE-TOP2A. (A) Western blot analysis was performed to determine protein expression levels of PBX3, TOP2A, PARP-1, and γ-H2AX. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+si-NC or Model+si-PBX3+OE-NC group; ns, not significant ( p ≥ 0.05). (B) IF staining was conducted to detect the DNA damage marker γ-H2AX. ∗∗∗ p < 0.001 vs. the Model+si-NC or Model+si-PBX3+OE-NC group; scale bars, 50 μm. (C) Cellular senescence was assessed using an SA-β-gal staining kit. ∗∗∗ p < 0.001 vs. the Model+si-NC or Model+si-PBX3+OE-NC group; scale bars, 50 μm. (D) ELISA was employed to measure the levels of degranulation markers β-hexosaminidase and histamine. ∗∗ p < 0.01, ∗∗∗ p < 0.001 vs. the Model+si-NC or Model+si-PBX3+OE-NC group. (E) Cytokine levels of IL-4, IL-5, and IFN-γ in cell supernatants were quantified by ELISA. ∗ p < 0.05, ∗∗∗ p < 0.001 vs. the Model+si-NC or Model+si-PBX3+OE-NC group. Data are represented as mean ± SEM ( n = 3 per group) from independent biological replicates. One-way ANOVA with Tukey’s post hoc correction for (A–E).

Article Snippet: Cells were then incubated overnight at 4°C with a primary antibody against PARP-1 (PB9309, BOSTER, Pleasanton, CA, USA, 1:100).

Techniques: Western Blot, Expressing, Staining, Marker, Enzyme-linked Immunosorbent Assay

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: PARP-1 regulates cartilage degeneration in OA mice. a Genotypes, along with mRNA and protein expression levels of PARP-1, were evaluated in primary cultured chondrocytes isolated from WT and PARP-1 KO mice. b Immunostaining for PARP-1 was performed on the cartilage and synovium of WT and PARP-1 KO mice. Represented data of ( a )( b ) were collected from biological triplicate. c Cartilage degeneration, erosion, and subchondral bone sclerosis/osteophyte formation were evaluated by Safranin-O staining. Quantification of the OARSI grade (d) , osteophyte maturity ( e ), osteophyte size ( f ), and subchondral bone plate thickness ( g ) are presented. h Synovitis was analyzed using hematoxylin and eosin staining. i Quantification of synovitis is shown. WT ( n = 10) or PARP-1 KO ( n = 17) mice were used. All values, derived from the Mann–Whitney U test, are expressed as the mean ± standard error of the mean. Safranin O-stained images of the joint sections are presented, illustrating the whole joint (50X), subchondral bone sclerosis/osteophyte size (100X), and cartilage and synovium (200X). Scale bar: 50 μm. Abbreviations: WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; OARSI, Osteoarthritis Research Society International

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Expressing, Cell Culture, Isolation, Immunostaining, Staining, Derivative Assay, MANN-WHITNEY, Knock-Out

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: Expression of PARP-1 and its effects on cartilage degeneration in WT and PARP-1 KO. a Expression of PARP-1 was analyzed in cartilage and synovium tissue from WT and PARP-1 KO. Represented images were collected from biological triplicate. TUNEL assay was performed to assess apoptosis in the cartilage ( b ) and synovium ( d ) of WT and PARP-1 KO mice. Quantification of apoptotic cells in cartilage ( c , n = 7) and synovium ( e , n = 4) were presented. All values, derived from the two-tailed Student’s t-test, are expressed as the mean ± standard error of the mean. Scale bar: 50 μm. Abbreviations: WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Expressing, TUNEL Assay, Derivative Assay, Two Tailed Test, Knock-Out

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: Genetic or pharmaceutical inhibition of PARP-1 increases apoptosis in primary cultured chondrocytes. a MTT assay was performed to evaluate the effect of CHX and 3-AB on chondrocyte viability ( n = 8). Chondrocytes were treated with CHX (25–100 µM), and 3-AB (100 µM) for 24 h. TUNEL assay was performed in primary cultured chondrocytes treated with CHX (50 µM) and 3-AB (100 µM) ( b ), with quantification results presented ( c , n = 6). Western blot analysis was also performed ( d ). Flow cytometry assay with PI/Annexin V was performed in primary cultured chondrocytes treated with CHX (50 µM) and 3-AB (100 µM) ( e ), with quantification results presented ( f , n = 8). Also, PI/Annexin V assay was performed in primary cultured chondrocytes from WT and PARP-1 KO treated with CHX ( g ), and quantification results were shown ( h , n = 8). TUNEL assay was performed in primary cultured chondrocytes from WT and PARP-1 KO treated with CHX ( i ), and quantification results were shown ( j , n = 6). Protein levels of PAPR-1, PAR, and c-caspase-3 were analyzed by Western blotting ( k ). Inflammasome-related factors, including NLRP3, caspase-1, and IL-1β, were also assessed ( l ). Western blotting data were collected from biological triplicate. All values, derived from the two-tailed Student’s t-test, are expressed as the mean ± standard error of the mean. Abbreviations: MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; CHX, cycloheximide; 3-AB, 3-aminobenzamide; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling; WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; PAR, poly ADP-ribose; c-caspase-3, cleaved caspase-3; NLRP3, nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 3; IL-1β, interleukin-1 beta

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Inhibition, Cell Culture, MTT Assay, TUNEL Assay, Western Blot, Flow Cytometry, Annexin V Assay, Derivative Assay, Two Tailed Test, Knock-Out, Binding Assay

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: Effect of PARP-1 KO on inflammatory factor-induced expression of anabolic and catabolic factors in chondrocytes. WT and PARP-1 KO chondrocytes were treated with IL-1β ( a ), TNF-α ( b ), IL-6 ( c ), and LPS ( d ) for 24 h. The mRNA expression levels of Sox9, Col2a1, Aggrecan, Mmp3, Mmp13, and Adamts5 were analyzed using conventional RT-PCR, with GADPH serving as an internal control. Represented images were collected from biological triplicate. Abbreviations: WT, wild-type; KO, knockout; IL-1β, interleukin-1 beta; TNF-α, tumor necrosis factor-alpha; IL-6, interleukin-6; LPS, lipopolysaccharide; Sox9, SRY-box transcription factor 9; Col2a1, collagen type II alpha 1 chain; Aggrecan, aggrecan proteoglycan; Mmp3, matrix metalloproteinase 3; Mmp13, matrix metalloproteinase 13; Adamts5, a disintegrin and metalloproteinase with thrombospondin motifs 5; RT-PCR, reverse transcription polymerase chain reaction; and GAPDH, glyceraldehyde 3-phosphate dehydrogenase

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Control, Knock-Out, Reverse Transcription, Polymerase Chain Reaction

Journal: Translational Oncology

Article Title: Poly-ADP-ribosylation modulated by poly(ADP-ribose) polymerase 1 is associated with glucose metabolism in colorectal cancer cells

doi: 10.1016/j.tranon.2025.102623

Figure Lengend Snippet: Inhibitory effect of 5-AIQ on PARP1 activation and cancer cell viability. A) Immunohistochemical staining confirmed that the expression of PAR polymer in colorectal cancer tissues was higher than that in normal tissues in 6 pairs of clinical samples (immunohistochemistry staining, original magnification ×400, scale bar = 100 μm). B) Database analysis of PARP1 expression in colorectal cancer and adjacent normal tissues. C) Colorectal cancer cells Caco-2 and LoVo were treated with 0–900 μM 5-AIQ, and their viability was assessed with CCK-8 assay. D) Western blots show PAR polymer levels in the cells, representing PARP1 activation. Densitometric analysis of the bands signifying E) the PAR/β-actin ratio in Caco-2 cells and F) the PAR/β-actin ratio in LoVo cells was performed with Quantity One software. * P < 0.05.

Article Snippet: Primary antibody against PARP1 was purchased from Santa Cruz Biotechnology, Inc (Santa Cruz, CA, USA), while primary antibodies against p-mTOR, GLUT-1, and HIF-1α were purchased from Proteintech Group (Rosemont, IL, USA).

Techniques: Activation Assay, Immunohistochemical staining, Staining, Expressing, Polymer, Immunohistochemistry, CCK-8 Assay, Western Blot, Software

Journal: Translational Oncology

Article Title: Poly-ADP-ribosylation modulated by poly(ADP-ribose) polymerase 1 is associated with glucose metabolism in colorectal cancer cells

doi: 10.1016/j.tranon.2025.102623

Figure Lengend Snippet: Relationship between Warburg effect and PARP1-modulated poly-ADP-ribosylation in colorectal cancer cells. A) The Warburg effect in cancer cells refers to increased glucose uptake and glycolysis to form lactate. The conversion of pyruvate to lactate is coupled with the oxidation of NADH to NAD + . Cancer cells upregulate glycolysis to increase NAD + regeneration for Poly-ADP-ribosylation during tumor progression. B) Inhibiting PARP1 reduces the depletion of intracellular NAD + , rendering it available for glycolysis and increasing the NAD + /NADH ratio. Blocking the additional NAD + consumption could disrupt the Warburg effect in colorectal cancer cells through the AKT/mTOR/HIF-1α pathway.

Article Snippet: Primary antibody against PARP1 was purchased from Santa Cruz Biotechnology, Inc (Santa Cruz, CA, USA), while primary antibodies against p-mTOR, GLUT-1, and HIF-1α were purchased from Proteintech Group (Rosemont, IL, USA).

Techniques: Blocking Assay