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Cell Signaling Technology Inc cytochrome c oxidase subunit 4
Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.
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Biodex Medical isokinetic dynamometer 4
Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.
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Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.
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Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.
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Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.
Invivomab Anti Mouse 4 1bb, supplied by Bio X Cell, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Macklin Inc hydrophobic fe 3 o 4 nanoparticles nps
Synthesis and Characterization of Chiral Fe 3 O 4 /GelMA Hydrogels. (A) Synthesis procedure of chiral Fe 3 O 4 /GelMA hydrogels. (B) SEM image (scale bar: 30 μm, 30 nm) of bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (C) UV-vis, (D) XRD spectra, and (E) CD spectra of bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. FT-IR spectra of (F1) L-cysteine and D-cysteine, and (F2) bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (G1-3) Fe 2p XPS spectra of bare Fe₃O₄, D‑Fe₃O₄, and L‑Fe₃O₄ nanoparticles. (H) Zeta potential of Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (I) Loading content of Fe 3 O 4 SPs in FG, D-FG and L-FG groups. (J1-2) General view and SEM cross-section view of the GelMA, Fe 3 O 4 /GelMA, D-Fe 3 O 4 /GelMA, L-Fe 3 O 4 /GelMA hydrogel (scale bar: 100 μm). (K1-2) Elemental spectrum analysis of chiral Fe 3 O 4 /GelMA hydrogel shows the presence of carbon (C), nitrogen (N), oxygen (O), sulfur (S), and iron (Fe). (L)The photocurable property of chiral hydrogels. (M) Degradation profile and (N) Swelling rate of the chiral Fe 3 O 4 /GelMA hydrogel. (O) Maximum compressive strength of chiral hydrogels. (P1-2) pH value and Zeta potential during degradation. (Q) Storage modulus (G′) and loss modulus (G″) versus frequency of chiral hydrogels. (n = 3, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001). Abbreviation: SPs, superparticles; SEM, scanning electron microscopy; UV–vis, ultraviolet–visible; XRD, X-ray diffraction; CD, circular dichroism; FT-IR, Fourier-transform infrared spectroscopy.
Hydrophobic Fe 3 O 4 Nanoparticles Nps, supplied by Macklin Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.

Journal: Journal of Sport and Health Science

Article Title: Influence of diet-induced obesity and voluntary exercise training on cardiac lipids and mitochondrial function in mice

doi: 10.1016/j.jshs.2025.101095

Figure Lengend Snippet: Voluntary exercise alters left ventricle gene and protein expression related to mitochondrial biogenesis and dynamics in high fat- and chow-fed mice. (A) Western blot analysis to assess purity of crude mitochondria isolation where left ventricle mitochondrial pellet expresses mitochondrial marker TOM70 and COXIV and supernatant expresses calnexin. Protein expression of (B) LCLAT1 and (C) MFN2 in left ventricle-isolated crude mitochondria and (D) LCLAT1, (E) PGC-1α, and (F) MFN2 in left ventricle tissue from male VET or sedentary mice fed an HFD or chow diet. Left ventricle mRNA expression of (G) OPA1 and (H) DRP1 in male VET or sedentary mice fed an HFD or chow diet. Values were calculated relative to 18S housekeeper. Calnexin and β-actin were used as internal controls of protein loading in left ventricle samples and COXIV as internal control of protein loading in crude mitochondria samples. Analysis was performed using two-way analysis of variance with Tukey’s post hoc test for multiple comparisons. Data are expressed as mean ± standard error of the mean. (B–C) n : 5–6 per group. (D–F) n = 7 per group. (G and H) n = 9 per group. CE = chow exercise; CS = chow sedentary; COXIV = cytochrome c oxidase subunit 4; DRP1 = dynamin-related protein 1; HE = high fat diet exercise; HFD = high fat diet; HS = high fat diet sedentary; LCLAT1 = lysocardiolipin acyltransferase 1; MFN2 = mitofusin-2; OPA1 = optic atrophy 1; PGC-1α = peroxisome proliferator-activated receptor gamma coactivator-1α; TOM70 = translocase of outer mitochondria membrane 70; VET = voluntary exercise training.

Article Snippet: Immunoblotting was performed with antibodies against lysocardiolipin acyltransferase 1(LCLAT1, PA5-25627; Thermo Fisher Scientific), PGC-1α (ab191838; Abcam, Cambridge, UK), MFN2 (PA5-118059; Thermo Fisher Scientific), ANP (sc-18811; Santa Cruz, Dallas, TX, USA), tumor necrosis factor alpha (TNFα, 3707; Cell Signaling, Danvers, MA, USA), phosphorylated adenosine monophosphate-activated protein kinase (AMPK, 2531; Cell Signaling), AMPKα (2532; Cell Signaling), Perilipin 5 (PA1-46215; Thermo Fisher Scientific), translocase of outer mitochondria membrane 70 (TOM70, 65675; Cell Signaling), cytochrome c oxidase subunit 4 (COXIV, 4844; Cell Signaling), and calnexin (208880; Merck, Rahway, NJ, USA).

Techniques: Expressing, Western Blot, Isolation, Marker, Control, Membrane

Synthesis and Characterization of Chiral Fe 3 O 4 /GelMA Hydrogels. (A) Synthesis procedure of chiral Fe 3 O 4 /GelMA hydrogels. (B) SEM image (scale bar: 30 μm, 30 nm) of bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (C) UV-vis, (D) XRD spectra, and (E) CD spectra of bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. FT-IR spectra of (F1) L-cysteine and D-cysteine, and (F2) bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (G1-3) Fe 2p XPS spectra of bare Fe₃O₄, D‑Fe₃O₄, and L‑Fe₃O₄ nanoparticles. (H) Zeta potential of Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (I) Loading content of Fe 3 O 4 SPs in FG, D-FG and L-FG groups. (J1-2) General view and SEM cross-section view of the GelMA, Fe 3 O 4 /GelMA, D-Fe 3 O 4 /GelMA, L-Fe 3 O 4 /GelMA hydrogel (scale bar: 100 μm). (K1-2) Elemental spectrum analysis of chiral Fe 3 O 4 /GelMA hydrogel shows the presence of carbon (C), nitrogen (N), oxygen (O), sulfur (S), and iron (Fe). (L)The photocurable property of chiral hydrogels. (M) Degradation profile and (N) Swelling rate of the chiral Fe 3 O 4 /GelMA hydrogel. (O) Maximum compressive strength of chiral hydrogels. (P1-2) pH value and Zeta potential during degradation. (Q) Storage modulus (G′) and loss modulus (G″) versus frequency of chiral hydrogels. (n = 3, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001). Abbreviation: SPs, superparticles; SEM, scanning electron microscopy; UV–vis, ultraviolet–visible; XRD, X-ray diffraction; CD, circular dichroism; FT-IR, Fourier-transform infrared spectroscopy.

Journal: Bioactive Materials

Article Title: Chiral Fe 3 O 4 /GelMA hydrogels regulate the osteoimmune microenvironment via Itgb3-mediated macrophage polarization to combat peri-implantitis

doi: 10.1016/j.bioactmat.2026.03.055

Figure Lengend Snippet: Synthesis and Characterization of Chiral Fe 3 O 4 /GelMA Hydrogels. (A) Synthesis procedure of chiral Fe 3 O 4 /GelMA hydrogels. (B) SEM image (scale bar: 30 μm, 30 nm) of bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (C) UV-vis, (D) XRD spectra, and (E) CD spectra of bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. FT-IR spectra of (F1) L-cysteine and D-cysteine, and (F2) bare Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (G1-3) Fe 2p XPS spectra of bare Fe₃O₄, D‑Fe₃O₄, and L‑Fe₃O₄ nanoparticles. (H) Zeta potential of Fe 3 O 4 SPs, D-Fe 3 O 4 SPs and L-Fe 3 O 4 SPs. (I) Loading content of Fe 3 O 4 SPs in FG, D-FG and L-FG groups. (J1-2) General view and SEM cross-section view of the GelMA, Fe 3 O 4 /GelMA, D-Fe 3 O 4 /GelMA, L-Fe 3 O 4 /GelMA hydrogel (scale bar: 100 μm). (K1-2) Elemental spectrum analysis of chiral Fe 3 O 4 /GelMA hydrogel shows the presence of carbon (C), nitrogen (N), oxygen (O), sulfur (S), and iron (Fe). (L)The photocurable property of chiral hydrogels. (M) Degradation profile and (N) Swelling rate of the chiral Fe 3 O 4 /GelMA hydrogel. (O) Maximum compressive strength of chiral hydrogels. (P1-2) pH value and Zeta potential during degradation. (Q) Storage modulus (G′) and loss modulus (G″) versus frequency of chiral hydrogels. (n = 3, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001). Abbreviation: SPs, superparticles; SEM, scanning electron microscopy; UV–vis, ultraviolet–visible; XRD, X-ray diffraction; CD, circular dichroism; FT-IR, Fourier-transform infrared spectroscopy.

Article Snippet: First, hydrophobic Fe 3 O 4 nanoparticles (NPs) (≥99.5%, 100 nm,C12834835, Macklin, Shanghai) were dispersed in n-hexane solvent, with amphiphilic sodium dodecyl sulfate (SDS, ≥99.0%, Sigma-Aldrich, #436143) as a surfactant and water, to form an oil-in-water emulsion under rapid stirring.

Techniques: Circular Dichroism, Zeta Potential Analyzer, Electron Microscopy, Fourier Transform Infrared Spectroscopy, Spectroscopy

Evaluation of the biocompatibility, antimicrobial efficacy, and multi-enzyme mimetic activities of chiral Fe 3 O 4 /GelMA hydrogels. (A, B) Cell viability analysis using the CCK-8 assay showed the total activity of RAW264.7 cells and MC3T3-E1 interacting with Fe 3 O 4 /GelMA composite hydrogel without changing the medium. (C) Live/Dead staining of RAW264.7 and MC3T3-E1 cells after 72 h of culture. (green: live cells; red: dead cells) Scale bar: 100 μm. (D) After co-culturing with GelMA, FG, D-FG, and L-FG hydrogels for 72 h, fluorescence images of RAW264.7 and MC3T3-E1 cells were captured. F-actin stained with rhodamine-phalloidin (red), and cell nuclei were stained with DAPI (blue). Scale bar: 100 μm. (E) Crystal violet staining of Pg bacterial biofilms treated with GelMA, FG, D-FG and L-FG groups. (F) Illustration of the multi-enzyme mimetic activities of chiral Fe 3 O 4 . (G1) The UV–vis absorbance spectra of Fe 3 O 4 +TMB + H 2 O 2 . (G2) Lineweaver-Burk double reciprocal plots of Fe 3 O 4 corresponding to H 2 O 2 . (H1) WTS-8 assay to determine •O 2 − scavenging activities. (H2) Scavenging rate of •O 2 − with different concentration of Fe 3 O 4 . (I1) H 2 O 2 scavenging activities of D-, L-, and LD-Fe 3 O 4 . (I2) H 2 O 2 scavenging rate of D-, L-, and LD-Fe 3 O 4 at different concentrations (0–100 μg/mL). Abbreviation: CCK-8, Cell Counting Kit-8; Pg, Porphyromonas gingivalis ; TMB, 3,3′,5,5′-tetramethylbenzidine; H 2 O 2 , hydrogen peroxide; WST-8, water-soluble tetrazolium salt-8; ROS, reactive oxygen species.

Journal: Bioactive Materials

Article Title: Chiral Fe 3 O 4 /GelMA hydrogels regulate the osteoimmune microenvironment via Itgb3-mediated macrophage polarization to combat peri-implantitis

doi: 10.1016/j.bioactmat.2026.03.055

Figure Lengend Snippet: Evaluation of the biocompatibility, antimicrobial efficacy, and multi-enzyme mimetic activities of chiral Fe 3 O 4 /GelMA hydrogels. (A, B) Cell viability analysis using the CCK-8 assay showed the total activity of RAW264.7 cells and MC3T3-E1 interacting with Fe 3 O 4 /GelMA composite hydrogel without changing the medium. (C) Live/Dead staining of RAW264.7 and MC3T3-E1 cells after 72 h of culture. (green: live cells; red: dead cells) Scale bar: 100 μm. (D) After co-culturing with GelMA, FG, D-FG, and L-FG hydrogels for 72 h, fluorescence images of RAW264.7 and MC3T3-E1 cells were captured. F-actin stained with rhodamine-phalloidin (red), and cell nuclei were stained with DAPI (blue). Scale bar: 100 μm. (E) Crystal violet staining of Pg bacterial biofilms treated with GelMA, FG, D-FG and L-FG groups. (F) Illustration of the multi-enzyme mimetic activities of chiral Fe 3 O 4 . (G1) The UV–vis absorbance spectra of Fe 3 O 4 +TMB + H 2 O 2 . (G2) Lineweaver-Burk double reciprocal plots of Fe 3 O 4 corresponding to H 2 O 2 . (H1) WTS-8 assay to determine •O 2 − scavenging activities. (H2) Scavenging rate of •O 2 − with different concentration of Fe 3 O 4 . (I1) H 2 O 2 scavenging activities of D-, L-, and LD-Fe 3 O 4 . (I2) H 2 O 2 scavenging rate of D-, L-, and LD-Fe 3 O 4 at different concentrations (0–100 μg/mL). Abbreviation: CCK-8, Cell Counting Kit-8; Pg, Porphyromonas gingivalis ; TMB, 3,3′,5,5′-tetramethylbenzidine; H 2 O 2 , hydrogen peroxide; WST-8, water-soluble tetrazolium salt-8; ROS, reactive oxygen species.

Article Snippet: First, hydrophobic Fe 3 O 4 nanoparticles (NPs) (≥99.5%, 100 nm,C12834835, Macklin, Shanghai) were dispersed in n-hexane solvent, with amphiphilic sodium dodecyl sulfate (SDS, ≥99.0%, Sigma-Aldrich, #436143) as a surfactant and water, to form an oil-in-water emulsion under rapid stirring.

Techniques: CCK-8 Assay, Activity Assay, Staining, Fluorescence, Concentration Assay, Cell Counting

Regulatory Effects of Chiral Hydrogels on the Bone Immune Microenvironment. (A, B) Immunofluorescence showed the expression of the M1 polarization marker CD86 (Green) and M2 polarization marker CD206 (Red) in GelMA, FG, L-FG and D-FG groups. Scale bar = 200 μm. (C, D) RT-qPCR results showing the expression of M1 polarization-associated factors Cd86 , Tnf , and Nos2 versus M2 polarization-associated factors Mrc1 , Arg1 , and Il10 in RAW264.7 cells after co-cultured with chiral Fe 3 O 4 /GelMA for 72 h. (E) Schematic of co-culture of RAW264.7 and MC3T3-E1 cells grown on hydrogel surfaces separated by a Transwell chamber. (F, G) Western Blot results showing the protein expression and quantification of CD206 and CD86 in RAW264.7 cells and (H, I) ALP and COL1 in MC3T3-E1 cells after co-cultured with chiral hydrogels. (J) Images of ALP staining on day 7 and 14 and (K) ARS staining on day 14 and 21. Scale bar = 200 μm. (n = 3, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001). Abbreviation: RT-qPCR, reverse transcription quantitative polymerase chain reaction; WB, Western blot; ALP, alkaline phosphatase; ARS, Alizarin Red S.

Journal: Bioactive Materials

Article Title: Chiral Fe 3 O 4 /GelMA hydrogels regulate the osteoimmune microenvironment via Itgb3-mediated macrophage polarization to combat peri-implantitis

doi: 10.1016/j.bioactmat.2026.03.055

Figure Lengend Snippet: Regulatory Effects of Chiral Hydrogels on the Bone Immune Microenvironment. (A, B) Immunofluorescence showed the expression of the M1 polarization marker CD86 (Green) and M2 polarization marker CD206 (Red) in GelMA, FG, L-FG and D-FG groups. Scale bar = 200 μm. (C, D) RT-qPCR results showing the expression of M1 polarization-associated factors Cd86 , Tnf , and Nos2 versus M2 polarization-associated factors Mrc1 , Arg1 , and Il10 in RAW264.7 cells after co-cultured with chiral Fe 3 O 4 /GelMA for 72 h. (E) Schematic of co-culture of RAW264.7 and MC3T3-E1 cells grown on hydrogel surfaces separated by a Transwell chamber. (F, G) Western Blot results showing the protein expression and quantification of CD206 and CD86 in RAW264.7 cells and (H, I) ALP and COL1 in MC3T3-E1 cells after co-cultured with chiral hydrogels. (J) Images of ALP staining on day 7 and 14 and (K) ARS staining on day 14 and 21. Scale bar = 200 μm. (n = 3, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001). Abbreviation: RT-qPCR, reverse transcription quantitative polymerase chain reaction; WB, Western blot; ALP, alkaline phosphatase; ARS, Alizarin Red S.

Article Snippet: First, hydrophobic Fe 3 O 4 nanoparticles (NPs) (≥99.5%, 100 nm,C12834835, Macklin, Shanghai) were dispersed in n-hexane solvent, with amphiphilic sodium dodecyl sulfate (SDS, ≥99.0%, Sigma-Aldrich, #436143) as a surfactant and water, to form an oil-in-water emulsion under rapid stirring.

Techniques: Immunofluorescence, Expressing, Marker, Quantitative RT-PCR, Cell Culture, Co-Culture Assay, Western Blot, Staining, Reverse Transcription, Real-time Polymerase Chain Reaction