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primary dermal fibroblast; normal, human, adult  (ATCC)


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    ATCC primary dermal fibroblast; normal, human, adult
    Primary Dermal Fibroblast; Normal, Human, Adult, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1908 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/dermal+fibroblasts/Primary+Dermal+Fibroblast%3B+Normal%2C+Human%2C+Adult/custom%40pcs-201-012%4042541731
    Average 99 stars, based on 1908 article reviews
    primary dermal fibroblast; normal, human, adult - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    In Vitro:

    Article Title: Biogenic Cu-Fe bimetallic nanoparticles induce apoptosis and inhibit invasion in glioblastoma cells.
    Article Snippet: 1 Faculty of Science, Department of Molecular Biology and Genetics, Erzurum Technical University, Erzurum, Türkiye 2 Erzurum Technical University, High Technology Application and Research Center (YUTAM), Erzurum, Turkey Abstract Background This study demonstrates the wide-ranging therapeutic potential of copper-iron (Cu–Fe) bimetallic nanoparticles (BNPs), which were synthesized using an environmentally friendly method involving Corylus avellana leaf extract.. Methods and Results Following phytochemical profiling of the aqueous extract via LC-MS/MS, the Cu–Fe BNPs were characterized and confirmed to be stable nanostructures with an average size of 20–30 nm.. Biological evaluations revealed selective cytotoxicity against U87-MG glioblastoma cells, with IC50 values of 11.8 μg/mL and 325 μg/mL for U87-MG and HDF cells respectively, resulting in a selectivity index (SI) of 27.54.

    MTT Assay:

    Article Title: Biogenic Cu-Fe bimetallic nanoparticles induce apoptosis and inhibit invasion in glioblastoma cells.
    Article Snippet: 1 Faculty of Science, Department of Molecular Biology and Genetics, Erzurum Technical University, Erzurum, Türkiye 2 Erzurum Technical University, High Technology Application and Research Center (YUTAM), Erzurum, Turkey Abstract Background This study demonstrates the wide-ranging therapeutic potential of copper-iron (Cu–Fe) bimetallic nanoparticles (BNPs), which were synthesized using an environmentally friendly method involving Corylus avellana leaf extract.. Methods and Results Following phytochemical profiling of the aqueous extract via LC-MS/MS, the Cu–Fe BNPs were characterized and confirmed to be stable nanostructures with an average size of 20–30 nm.. Biological evaluations revealed selective cytotoxicity against U87-MG glioblastoma cells, with IC50 values of 11.8 μg/mL and 325 μg/mL for U87-MG and HDF cells respectively, resulting in a selectivity index (SI) of 27.54.

    Article Title: Standardized Herbal Lozenges Containing <i>Schefflera leucantha</i> Extract: A Novel Approach for Respiratory Health Support
    Article Snippet: .. The cytotoxicity of the selected S. leucantha extract and the final formulated lozenges was evaluated using the MTT colorimetric assay20 on human dermal fibroblasts (ATCC CRL-2076; Manassas, Virginia, USA). ..

    Generated:

    Article Title: BARCODE: high throughput screening and analysis of soft active materials
    Article Snippet: .. Data presented in Fig. were generated from source videos of human dermal fibroblasts (ATCC PCS-201-010), which we further processed as described below. ..

    Article Title: BARCODE: high throughput screening and analysis of soft active materials.
    Article Snippet: .. Preparation and imaging of cell monolayers Data presented in Fig. 5A-F were generated from source videos34 of human dermal fibroblasts (ATCC PCS-201-010), which we further processed as described below. ..

    Cell Culture:

    Article Title: Semaphorin 3A and 3F Promote Lumen Expansion in TIE2-Mutated Venous Malformation
    Article Snippet: Then, 0.625 U/mL of thrombin (Sigma, cat T4648) and 0.5-mL beads/fibrinogen suspension were carefully added to a well of a 24-well plate and incubated at 37 °C for 20 minutes to allow fibrin clotting. .. The gels were overlaid with human dermal fibroblasts (ATCC, cat PCS-201-012) at 2×104 cells/well and cultured in EC growth medium supplemented with 10% fetal bovine serum. ..

    Article Title: Nano-Encapsulated Spicule System Enhances Delivery of Wharton's Jelly MSC Secretome and Promotes Skin Rejuvenation: Preclinical and Clinical Evaluation.
    Article Snippet: Data were acquired and analyzed using a FACSVerseTM flow cytometer (BD Biosciences, Franklin Lakes, NJ, USA). .. Human keratinocytes (HaCaT; AddexBio, San Diego, CA, USA; T0020001) and dermal fibroblasts (HS68; ATCC, Manassas, VA, USA; CRL-1635) were cultured in Dulbecco’s Modified Eagle Medium (DMEM; Gibco, Thermo Fisher Scientific, Waltham, MA, USA), supplemented with 10% fetal bovine serum (FBS; Gibco) and 1% penicillin–streptomycin (Gibco). supplemented with 10% fetal bovine serum (FBS; Gibco) and 1% penicillin–streptomycin (Gibco). ..

    Modification:

    Article Title: Antibacterial Tellurium Dioxide Nanoparticles Incorporated into an Adhesive Wound Dressing.
    Article Snippet: .. Following ISO 10993 standards, various concentrations of PLAL TeO2 NPs were added to 1 mL of Dulbecco’s Modified Eagle Media (DMEM, Gibco) supplemented with 10% fetal bovine serum (FBS, Gibco) in a 12 well plate with primary dermal fibroblasts (ATCC PCS-201-012) seeded at 3 × 105 cells/sample in standard incubator conditions (5% CO2, humidified, 37 °C). ..

    Article Title: Nano-Encapsulated Spicule System Enhances Delivery of Wharton's Jelly MSC Secretome and Promotes Skin Rejuvenation: Preclinical and Clinical Evaluation.
    Article Snippet: Data were acquired and analyzed using a FACSVerseTM flow cytometer (BD Biosciences, Franklin Lakes, NJ, USA). .. Human keratinocytes (HaCaT; AddexBio, San Diego, CA, USA; T0020001) and dermal fibroblasts (HS68; ATCC, Manassas, VA, USA; CRL-1635) were cultured in Dulbecco’s Modified Eagle Medium (DMEM; Gibco, Thermo Fisher Scientific, Waltham, MA, USA), supplemented with 10% fetal bovine serum (FBS; Gibco) and 1% penicillin–streptomycin (Gibco). supplemented with 10% fetal bovine serum (FBS; Gibco) and 1% penicillin–streptomycin (Gibco). ..

    Imaging:

    Article Title: BARCODE: high throughput screening and analysis of soft active materials.
    Article Snippet: .. Preparation and imaging of cell monolayers Data presented in Fig. 5A-F were generated from source videos34 of human dermal fibroblasts (ATCC PCS-201-010), which we further processed as described below. ..



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    Biocompatibility of hydrogels. (A-C) Hydrogels were incubated in the respective cell culture media for 72 h, and the obtained extracts were used to assess their effects on the metabolic activity of huMECs (A), vSMCs (B), and <t>NHDFs</t> (C) after 48 h of culture. (D, E) Hydrogel extracts were added to primary human monocytes obtained from five independent donors. The differentiation efficiency of these immune cells into M1 (D) or M2 (E) macrophages was analyzed by flow cytometry using specific markers. (F) Anti-factor Xa activity of HA c and sHA c was determined in comparison with Hep using a chromogenic assay. (A-F) One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. (G) In-vivo assessment of GelMA and GelMA/sHA c hydrogels loaded with TIMP-3. Experimental overview: TIMP-3-loaded GelMA and GelMA/sHA c hydrogels were implanted subcutaneously into BALB/c mice for 14 days. (H) Representative histological images of explanted gels stained for MPO (neutrophils), CD68 (macrophages), CD31 (microvessels), and Sirius red (collagen deposition). The granulation tissue between the muscle tissue and the implant is highlighted by dotted yellow lines. (I-L) Quantification of MPO + and CD68 + cells, CD31 + events, and Sirius red intensity (three ROIs per sample). Statistical analysis was performed using an unpaired t -test with Welch's correction: ∗p < 0.05, ∗∗p < 0.01.
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    Biocompatibility of hydrogels. (A-C) Hydrogels were incubated in the respective cell culture media for 72 h, and the obtained extracts were used to assess their effects on the metabolic activity of huMECs (A), vSMCs (B), and <t>NHDFs</t> (C) after 48 h of culture. (D, E) Hydrogel extracts were added to primary human monocytes obtained from five independent donors. The differentiation efficiency of these immune cells into M1 (D) or M2 (E) macrophages was analyzed by flow cytometry using specific markers. (F) Anti-factor Xa activity of HA c and sHA c was determined in comparison with Hep using a chromogenic assay. (A-F) One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. (G) In-vivo assessment of GelMA and GelMA/sHA c hydrogels loaded with TIMP-3. Experimental overview: TIMP-3-loaded GelMA and GelMA/sHA c hydrogels were implanted subcutaneously into BALB/c mice for 14 days. (H) Representative histological images of explanted gels stained for MPO (neutrophils), CD68 (macrophages), CD31 (microvessels), and Sirius red (collagen deposition). The granulation tissue between the muscle tissue and the implant is highlighted by dotted yellow lines. (I-L) Quantification of MPO + and CD68 + cells, CD31 + events, and Sirius red intensity (three ROIs per sample). Statistical analysis was performed using an unpaired t -test with Welch's correction: ∗p < 0.05, ∗∗p < 0.01.
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    Image Search Results


    Biocompatibility of hydrogels. (A-C) Hydrogels were incubated in the respective cell culture media for 72 h, and the obtained extracts were used to assess their effects on the metabolic activity of huMECs (A), vSMCs (B), and NHDFs (C) after 48 h of culture. (D, E) Hydrogel extracts were added to primary human monocytes obtained from five independent donors. The differentiation efficiency of these immune cells into M1 (D) or M2 (E) macrophages was analyzed by flow cytometry using specific markers. (F) Anti-factor Xa activity of HA c and sHA c was determined in comparison with Hep using a chromogenic assay. (A-F) One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. (G) In-vivo assessment of GelMA and GelMA/sHA c hydrogels loaded with TIMP-3. Experimental overview: TIMP-3-loaded GelMA and GelMA/sHA c hydrogels were implanted subcutaneously into BALB/c mice for 14 days. (H) Representative histological images of explanted gels stained for MPO (neutrophils), CD68 (macrophages), CD31 (microvessels), and Sirius red (collagen deposition). The granulation tissue between the muscle tissue and the implant is highlighted by dotted yellow lines. (I-L) Quantification of MPO + and CD68 + cells, CD31 + events, and Sirius red intensity (three ROIs per sample). Statistical analysis was performed using an unpaired t -test with Welch's correction: ∗p < 0.05, ∗∗p < 0.01.

    Journal: Bioactive Materials

    Article Title: Glycosaminoglycan-functionalized hydrogels for sustained delivery of tissue inhibitor of metalloproteinase-3 mediating matrix metalloprotease inhibition and extracellular matrix stabilization

    doi: 10.1016/j.bioactmat.2026.02.010

    Figure Lengend Snippet: Biocompatibility of hydrogels. (A-C) Hydrogels were incubated in the respective cell culture media for 72 h, and the obtained extracts were used to assess their effects on the metabolic activity of huMECs (A), vSMCs (B), and NHDFs (C) after 48 h of culture. (D, E) Hydrogel extracts were added to primary human monocytes obtained from five independent donors. The differentiation efficiency of these immune cells into M1 (D) or M2 (E) macrophages was analyzed by flow cytometry using specific markers. (F) Anti-factor Xa activity of HA c and sHA c was determined in comparison with Hep using a chromogenic assay. (A-F) One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. (G) In-vivo assessment of GelMA and GelMA/sHA c hydrogels loaded with TIMP-3. Experimental overview: TIMP-3-loaded GelMA and GelMA/sHA c hydrogels were implanted subcutaneously into BALB/c mice for 14 days. (H) Representative histological images of explanted gels stained for MPO (neutrophils), CD68 (macrophages), CD31 (microvessels), and Sirius red (collagen deposition). The granulation tissue between the muscle tissue and the implant is highlighted by dotted yellow lines. (I-L) Quantification of MPO + and CD68 + cells, CD31 + events, and Sirius red intensity (three ROIs per sample). Statistical analysis was performed using an unpaired t -test with Welch's correction: ∗p < 0.05, ∗∗p < 0.01.

    Article Snippet: Normal human dermal fibroblasts (NHDFs) (PromoCell GmbH, Heidelberg, Germany), were cultured in Dulbecco's modified eagle medium (DMEM) with 10 % fetal calf serum (FCS) and 1 % streptomycin and penicillin at 37 °C at 80 % confluency in 175 cm 2 flasks.

    Techniques: Incubation, Cell Culture, Activity Assay, Flow Cytometry, Comparison, Chromogenic Assay, In Vivo, Staining

    TIMP-3 maintains protease inhibitory activity in the presence of sHA c and hydrogels release bioactive TIMP-3. (A-D) Influence of soluble GAGs and hydrogel extracts on TIMP-3-mediated inhibition of protease activity in TNF-α-stimulated NHDFs. (A) Schematic of the experimental design. Inflammation was modeled by stimulating NHDFs with TNF-α, inducing increased protease secretion. Gelatinase/collagenase activity in supernatants was quantified using the EnzChek assay with a fluorogenic gelatin substrate in the presence or absence of soluble TIMP-3, soluble GAGs or hydrogel extracts. (B) Protease activity in the supernatants after TNF-α treatment relative to unstimulated controls. (C) Protease activity of TNF-α-stimulated supernatants incubated with soluble GAGs (HA c , sHA c ) with or without TIMP-3. (D) Protease activity of TNF-α-stimulated supernatants incubated with hydrogel extracts (prepared by 72 h hydrogel incubation in medium) in the absence or presence of TIMP-3. One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. Only significant differences relative to the Ctrl without TIMP-3 or relative to TIMP-3 alone are shown in C/D. (E) The inhibitory potential of TIMP-3 released from the hydrogels was measured using a MMP-9 activity assay. (F) The ratio of bioactive TIMP-3 to the total amount of released TIMP-3 was calculated and expressed as a fold change relative to GelMA hydrogels without GAGs. (G) Collagen-based ECMs were incubated with collagenase (CHC) for 20 or 60 min with TIMP-3 released from the hydrogels after 24 or 168 h. The remaining collagen was detected after Sirius red staining and elution. Two-way ANOVA for A, B: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. One-way ANOVA for C: ∗p < 0.05. (H) Molecular rationale for the regulatory role of sHA c on TIMP-3-mediated protease inhibition. The MD-refined complex of TIMP-3 (in grey) with HA6_3AC1 (atom-colored brown sticks, color gradient as in D) is shown superimposed with the TIMP-3/ADAM complex (PDB ID 3CKI ). ADAM is shown in green, and the corresponding TIMP-3 structure has been omitted for clarity.

    Journal: Bioactive Materials

    Article Title: Glycosaminoglycan-functionalized hydrogels for sustained delivery of tissue inhibitor of metalloproteinase-3 mediating matrix metalloprotease inhibition and extracellular matrix stabilization

    doi: 10.1016/j.bioactmat.2026.02.010

    Figure Lengend Snippet: TIMP-3 maintains protease inhibitory activity in the presence of sHA c and hydrogels release bioactive TIMP-3. (A-D) Influence of soluble GAGs and hydrogel extracts on TIMP-3-mediated inhibition of protease activity in TNF-α-stimulated NHDFs. (A) Schematic of the experimental design. Inflammation was modeled by stimulating NHDFs with TNF-α, inducing increased protease secretion. Gelatinase/collagenase activity in supernatants was quantified using the EnzChek assay with a fluorogenic gelatin substrate in the presence or absence of soluble TIMP-3, soluble GAGs or hydrogel extracts. (B) Protease activity in the supernatants after TNF-α treatment relative to unstimulated controls. (C) Protease activity of TNF-α-stimulated supernatants incubated with soluble GAGs (HA c , sHA c ) with or without TIMP-3. (D) Protease activity of TNF-α-stimulated supernatants incubated with hydrogel extracts (prepared by 72 h hydrogel incubation in medium) in the absence or presence of TIMP-3. One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. Only significant differences relative to the Ctrl without TIMP-3 or relative to TIMP-3 alone are shown in C/D. (E) The inhibitory potential of TIMP-3 released from the hydrogels was measured using a MMP-9 activity assay. (F) The ratio of bioactive TIMP-3 to the total amount of released TIMP-3 was calculated and expressed as a fold change relative to GelMA hydrogels without GAGs. (G) Collagen-based ECMs were incubated with collagenase (CHC) for 20 or 60 min with TIMP-3 released from the hydrogels after 24 or 168 h. The remaining collagen was detected after Sirius red staining and elution. Two-way ANOVA for A, B: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. One-way ANOVA for C: ∗p < 0.05. (H) Molecular rationale for the regulatory role of sHA c on TIMP-3-mediated protease inhibition. The MD-refined complex of TIMP-3 (in grey) with HA6_3AC1 (atom-colored brown sticks, color gradient as in D) is shown superimposed with the TIMP-3/ADAM complex (PDB ID 3CKI ). ADAM is shown in green, and the corresponding TIMP-3 structure has been omitted for clarity.

    Article Snippet: Normal human dermal fibroblasts (NHDFs) (PromoCell GmbH, Heidelberg, Germany), were cultured in Dulbecco's modified eagle medium (DMEM) with 10 % fetal calf serum (FCS) and 1 % streptomycin and penicillin at 37 °C at 80 % confluency in 175 cm 2 flasks.

    Techniques: Activity Assay, Inhibition, Incubation, Staining