anti β actin  (Proteintech)

Journal: Food Chemistry: Molecular Sciences

Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen

doi: 10.1016/j.fochms.2026.100357

Figure Lengend Snippet: β-Gal detection of the association between its fusion partner Nb16 and Ara h 3 by ELISA. The utility of β-gal as a colorimetric enzyme in ELISA was assessed. Nb16-βgal association with Ara h 3 coated on the surface of the wells, but not with the control proteins, was detected. (A) SDS-PAGE analysis of Ara h 3 and control proteins used to coat the microplate. Nonreduced (lane 1) and reduced (lane 2) Ara h 3 were separated on a 4–12% SDS gel and stained with CBB. Chicken allergen Gal d 2 (lane 3) and cow's milk allergen Bos d 4 (lane 4) were included as control samples. The molecular masses (in kDa) of the proteins in the marker (lane M) are shown on the right side of the gel images. (B) The kinetic curves of the signal readout during plate incubation after the β-gal substrate ONPG was added. The black line shows the average signal of the wells incubated with TBS during the coating step. Red, green, and blue lines show the average signals of the wells coated with Gal d 2, Bos d 4, and Ara h 3, respectively. All the coating samples were at a concentration of 20 μg/mL. (C) A bar representation of β-gal detection in the ELISA experiment using the endpoint data. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: Milli-Q water was purified in-house using a Milli-Q Advantage A10 system (Millipore, Bedford, MA, USA) and used throughout. o -Nitrophenyl-β-galactoside (ONPG), Isopropyl β-D-1-thiogalactopyranoside (IPTG), Kanamycin (Kan), and X-Gal were purchased from GoldBio (St Louis, MO, USA).

Techniques: Enzyme-linked Immunosorbent Assay, Control, SDS Page, SDS-Gel, Staining, Marker, Incubation, Concentration Assay

Journal: Food Chemistry: Molecular Sciences

Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen

doi: 10.1016/j.fochms.2026.100357

Figure Lengend Snippet: Detection of peanut allergen Ara h 3 at various concentrations. (A) Plate wells were coated with Ara h 3 at the concentrations indicated below the bar plot. Results were analyzed as described in C, but without background (signal for [Ara h 3] = 0) correction. (B) Kinetic signal readout during plate incubation after the β-gal substrate ONPG was added. Ara h 3 concentrations are indicated next to the endpoint signals. (C) The slopes of the linear fit to the kinetic data are shown in a bar graph. The Ara h 3 concentrations in the coating samples are indicated under the bars. (D) The slope of the kinetic data as a function of the Ara h 3 concentration is shown. The red straight line shows the results of fitting the data for Ara h 3 concentrations <2.5 μg/mL. (E) A semi-log plot of the slopes of the β-gal signal against the Ara h 3 concentration. The red sigmoidal line shows the result of a four-parameter logistic curve fit. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: Milli-Q water was purified in-house using a Milli-Q Advantage A10 system (Millipore, Bedford, MA, USA) and used throughout. o -Nitrophenyl-β-galactoside (ONPG), Isopropyl β-D-1-thiogalactopyranoside (IPTG), Kanamycin (Kan), and X-Gal were purchased from GoldBio (St Louis, MO, USA).

Techniques: Incubation, Concentration Assay

Journal: Food Chemistry: Molecular Sciences

Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen

doi: 10.1016/j.fochms.2026.100357

Figure Lengend Snippet: Direct ELISA detection of peanut proteins in baked food. Kinetic signal readout during plate incubation with β-gal substrate ONPG. Each data point is the average of three triplicate wells. Data obtained by coating the plate with diluted muffin extract at peanut protein concentrations of 1.56, 3.13, 6.25, 15.63, and 39.06 ppm are shown in red, green, blue, cyan, and magenta, respectively. Data for the negative control, with wells treated with TBS during coating, are shown in black. Linear fits were applied to each data set, and the y-axis intercept of each fit was subtracted from each data point to shift the data set vertically. The straight lines are the results of linear fits of the shifted data. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: Milli-Q water was purified in-house using a Milli-Q Advantage A10 system (Millipore, Bedford, MA, USA) and used throughout. o -Nitrophenyl-β-galactoside (ONPG), Isopropyl β-D-1-thiogalactopyranoside (IPTG), Kanamycin (Kan), and X-Gal were purchased from GoldBio (St Louis, MO, USA).

Techniques: Direct ELISA, Incubation, Negative Control

Journal: Materials Today Bio

Article Title: Ultrasound-responsive CPS piezoelectric hydrogel synergistically repairs annulus fibrosus defects through immune reprogramming and cell recruitment

doi: 10.1016/j.mtbio.2026.102825

Figure Lengend Snippet: Assessment of the anti-inflammatory capacity of CPS gel in vitro . A Schematic of the co-culture of hydrogel with RAW 264.7. B Quantification of the relative fluorescence intensity of TNF-α. C Quantification of the relative fluorescence intensity of IL-1β. D Immunofluorescence image of TNF-α expression in RAW 264.7 (Scale bar = 50 μm). E Immunofluorescence image of IL-1β expression in RAW 264.7 (Scale bar = 50 μm). F-H The protein expression level of TNF-α and IL-1β was evaluated by WB and quantified by ImageJ. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Staining was performed using IL-1β (Bioss, BS-0812R) and TNF-α (Santa, SC-52746) probes, and the staining was observed under a fluorescent inverted microscope.

Techniques: In Vitro, Co-Culture Assay, Fluorescence, Immunofluorescence, Expressing

Journal: Materials Today Bio

Article Title: Ultrasound-responsive CPS piezoelectric hydrogel synergistically repairs annulus fibrosus defects through immune reprogramming and cell recruitment

doi: 10.1016/j.mtbio.2026.102825

Figure Lengend Snippet: In vivo study of CPS gel for AF repair. A H&E, S&O staining sections of rat IVD at 4W and 8W post-operation (scale bar = 1 mm). B Col-1, IL-1β IHC staining sections of rat IVD at 4W and 8W post-operation (Scale bar = 50 μm). C Postoperative 4W Col-1 quantitative analysis. D Postoperative 8W Col-1 quantitative analysis. E. Postoperative 4W IL-1β quantitative analysis. F Postoperative 8W IL-1β quantitative analysis. Data are mean ± SD (n = 3). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Staining was performed using IL-1β (Bioss, BS-0812R) and TNF-α (Santa, SC-52746) probes, and the staining was observed under a fluorescent inverted microscope.

Techniques: In Vivo, Staining, Immunohistochemistry

Journal: International Dental Journal

Article Title: Meis1 Negatively Regulates Epithelial-Mesenchymal Transition via Wnt/β-catenin Pathway in Oral Submucous Fibrosis

doi: 10.1016/j.identj.2025.109323

Figure Lengend Snippet: Meis1 regulated EMT through the Wnt/β-catenin pathway. ( A ) q-PCR analysis of Meis1 knockdown efficiency in HaCaT cells transfected with sh-Meis1 plasmids, ** P < .01. ( B ) Western blot analysis of Meis1 knockdown efficiency in HaCaT cells transfected with sh-Meis1 plasmids. ( C ) Western blot analysis of lentivirus-mediated Meis1 knockdown efficiency by shRNA in HaCaT cells. ( D ) Venn diagram showing overlapping differentially expressed genes (DEGs) between the TGF-β1-induced group and sh-Meis1-2 group (C1: the control group; C2: TGF-β1-induced group; C3: sh-Meis1-2 group). ( E ) Pathway enrichment analysis of overlapping DEGs between the TGF-β1-induced group and sh-Meis1-2 group. ( F-H ) q-PCR analysis of β-catenin, cyclin D1, and c-Myc mRNA expression in cells with Meis1 overexpression, * P < .05, ** P < .01. ( I ) Western blot analysis of β-catenin, c-Jun, c-Myc, and cyclin D1 protein expression in cells with Meis1 overexpression. ( J-L ) q-PCR analysis of β-catenin, cyclin D1, and c-Myc mRNA expression in cells with Meis1 knockdown, * P < .05, ** P < .01. ( M ) Western blot analysis of β-catenin, c-Jun, c-Myc, and cyclin D1 protein expression in cells with Meis1 knockdown. ( N ) Western blot analysis of β-catenin protein expression in cells with or without MSAB treatment. ( O ) Western blot analysis of α-SMA, Vimentin, E-cadherin, and N-cadherin protein expression in cells with or without MSAB treatment.

Article Snippet: MSAB was used to treat HaCaT cells by blocking the Wnt/β-catenin pathway (MCE, HY-120697).

Techniques: Knockdown, Transfection, Western Blot, shRNA, Control, Expressing, Over Expression

Journal: Bioactive Materials

Article Title: Bacteria-responsive DNAgel system for targeted delivery of photothermally enhanced MXene/MoS 2 in the treatment of pyogenic osteomyelitis

doi: 10.1016/j.bioactmat.2025.10.023

Figure Lengend Snippet: MXMoS 2 activates Wnt signaling pathways to promote osteogenic differentiation and enhance bone regeneration. (A) GO pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (B) KEGG pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (C) Heatmap of inflammation-related gene expression. (D) GSEA of GO analysis in the experimental and control groups, demonstrating pathways such as osteoblast differentiation, regulation of macrophage activation, cell adhesion, positive regulation of cell migration,cell-cell junction. (E) PPI analyses identifying four distinct gene clusters (modules). (F) Bubble chart showed the various network topology metrics for the 4 modules weighted and quantified to obtain an overall score. (G) GO analysis of the genes in module 2 showed that they are associated with osteoblast differentiation and the Wnt signaling pathway. (H) Box plot of representative Wnt signaling pathway genes significantly upregulated in the MXMoS 2 group. (I) The six genes mentioned above were predicted for their upstream transcription factor regulation. (J) Schematic illustration of the mechanism of MXMoS 2 regulating macrophage polarization. (K) Representative Western blot images of WNT4 and β-Catenin expression in control group (LPS), MXMoS 2 group (LPS + MXMoS 2 ) and MXMoS 2 +siRNA group (LPS + MXMoS 2 +siRNA-WNT4). (L – M) Quantification of WNT4 and β-Catenin protein levels corresponding to (K) . ∗∗p < 0.01, ∗∗∗p < 0.001, and ∗∗∗∗p < 0.0001.

Article Snippet: Primary antibodies for immunocytochemistry and immunofluorescence staining—including ARG1 and iNOS, TRAP, β-Catenin, OCN and WNT4—were obtained from Proteintech (China).

Techniques: Protein-Protein interactions, Control, Gene Expression, Activation Assay, Migration, Western Blot, Expressing