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c2c12 myoblasts (ATCC)

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ATCC c2c12 myoblasts
C2c12 Myoblasts, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 8620 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c2c12+myoblasts/C2C12/pm42319790-25-14-19
Average 99 stars, based on 8620 article reviews

c2c12 myoblasts - by Bioz Stars, 2026-10

99/100 stars

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Modification:

Article Title: Sporoderm Disruption Reshapes the Chemical Characteristics and Enhances the Mitochondrial Protective Activity of Ganoderma lucidum Spore Polysaccharides via SIRT1/AMPK Signaling.
Article Snippet: .. C2C12 myoblasts (American Type Culture Collection, ATCC) were grown in highglucose Dulbecco’s Modified Eagle Medium (DMEM), supplemented with 10% heatinactivated fetal bovine serum (FBS) and 1% penicillin/streptomycin (P/S), in a humidified https://doi.org/10.3390/ijms27114741 incubator at 37 ◦C with 5% CO2. ..

Article Title: Engineered Muscle Tissue Analysis of Irisin Protection Against Glucocorticoid- and Cancer Cachexia-Induced Muscle Wasting and Cardiotoxicity
Article Snippet: .. C2C12 myoblasts (ATCC, CRL-1772) were expanded in growth media consisting of 10% (v/v) fetal bovine serum (Gibco 16140-071) and 100 U/mL penicillin (Sigma P7794100MU) in high-glucose Dulbecco’s Modified Eagle Medium (DMEM; Gibco 11995-065). .. Differentiation media 1 3 comprised 2% (v/v) horse serum (Gibco 26050-088) and 100 U/mL penicillin in low-glucose DMEM (Gibco 11885-084).

Article Title: Oxidative Stress and Diminished Mitochondrial Proteostatic Reserve Are Linked to Enhanced mtUPR Initiation in Aged Mouse Muscle.
Article Snippet: .. HEK 293 T cells and C2C12 myoblasts were purchased from ATCC (#CRL- 3216, #CRL- 1772) and cultured subconfluently at 37°C in 5% CO2 in high glucose Dulbecco's modified Eagle's media (DMEM; #10- 017- CV; Corning Life Sciences) containing 10% fetal bovine serum (FBS; #30- 2020; ATCC) and 1% penicillin–streptomycin (PS; #15140122; Thermo Fisher Scientific). .. C2C12 myoblasts were seeded onto plates precoated with a 2D type I rat tail collagen matrix (#5153- 1KIT; Advanced Biomatrix) as described (Laskin, Steiner, et al. 2025).

Article Title: Bacteroides-derived endocannabinoid-like commendamide attenuates skeletal muscle ferroptosis in vitro: implications for Duchenne muscular dystrophy.
Article Snippet: Analyst software 124 (version 1.5.2; ABSciex) was used for data recording and Multiquant software (version 2.0.2; ABSciex) for 125 quantitative analyses. .. 126 2.4 Cell Culture and Reagents 127 Murine C2C12 myoblasts were purchased from ATCC (cat. no. CRL-1772) and propagated in growth medium 128 (GM) consisting of Dulbecco’s Modified Eagle’s Medium (DMEM; cat. no. 11995065, Life Technologies) 129 supplemented with 10% fetal bovine serum (FBS; cat. no. 16000044, Life Technologies), 5000 U/mL penicillin and 130 5000 μg/mL streptomycin (cat. no. 15070063, Life Technologies), and 1% L-glutamine (cat. no. A2916801, Life 131 Technologies). .. To induce differentiation into myotubes, proliferating C2C12 cells were switched to differentiation 132 medium (DM), composed of DMEM supplemented with 0.1% fetal bovine serum (FBS; cat. no. 16000044, Life 133 Technologies), 5000 U/mL penicillin and 5000 μg/mL streptomycin (cat. no. 15070063, Life Technologies), and 134 1% L-glutamine (cat. no. A2916801, Life Technologies) plus 1% Insulin-Transferrin-Selenium (ITS -G; cat. no. 135 41400045 Life Technologies) for three days.

Cell Culture:

Article Title: Targeting FoxO1/3a, NF-κB, and mTOR signaling attenuates muscle atrophy in sepsis.
Article Snippet: .. C2C12 myoblasts were obtained from ATCC (Cat# CRL-1772) and cultured in DMEM (Gibco, Cat# 11965092) with 10% FBS (Gibco, Cat# 10099141). .. Differentiation into myotubes was induced by switching to 2% horse serum (Gibco, Cat# 16050122).

Synthesized:

Article Title: Poly(sulfobetaine- co -oligoethylene Glycol Methyl Ether Methacrylate) Copolymers with Improved Anti-Fouling and Anti-Coagulant Properties.
Article Snippet: Zwitterionic polymers such as poly(sulfobetaines) and polyether polymers such as poly(ethylene glycol) (PEG) have both been reported as effective antifouling materials for various biomedical applications based on their high-waterbinding capacities through hydrogen bonding (PEG) or ion−dipole interactions (zwitterionic polymers).. Herein, to assess whether synergistic antifouling properties can be achieved when poly(sulfobetaine) and PEG moieties are combined into a single polymer, linear copolymers were fabricated by the chain transfer radical copolymerization of [2-(methacryloyloxy) ethyl] dimethyl-(3-sulfopropyl) ammonium hydroxide (DMAPS) and oligo(ethylene glycol) methyl ether methacrylate (OEGMA) together with a functional comonomer that introduced an aldehyde or hydrazide functional group to enable in situ gelation via hydrazone cross-linking.. In general, hydrogels prepared with more OEGMA showed longer gelation times, increased protein uptake (because of their higher degree of swelling), and faster plasma clotting times.

Image Search Results

Preferential silencing of ACVR1 R206H in FOP patient-derived fibroblasts using LNA and MOE gapmers (A) Sequence alignment showing LNA and MOE gapmer binding sites spanning the ACVR1 c.617G>A mutation (R206H). Mismatches are shown in lowercase; green: ACVR1 WT variant; red: ACVR1 R206H variant. (B) Schematic overview of the experimental timeline: day 2, cell revival; day 0, seeding; day 1, transfection; day 3, RNA/protein harvest. Toxicity assessments were performed at 4, 12, 24, and 48 h post-transfection. (C and D) RT-qPCR analysis of total ACVR1 mRNA levels following treatment with 100 nM (C) or 10 nM (D) gapmers. (E) Representative immunoblots showing total ACVR1 protein levels post-treatment with 100 and 10 nM gapmers. GAPDH served as a loading control. (F and G) Quantification of total ACVR1 protein abundance relative to healthy control cells at 100 nM (F) and 10 nM (G) using densitometric analysis of the immunoblot images (E). (H–K) Allele-specific RT-qPCR quantification of ACVR1 WT (H, J) and ACVR1 R206H (I, K) transcript levels following treatment with 100 nM (H, I) or 10 nM (J, K) gapmers. (L) Representative immunoblots of V5-tagged ACVR1 WT and ACVR1 R206H proteins expressed in C2C12 cells 48 h post-treatment with 10 nM gapmers, with GAPDH as a loading control. (M and N) Densitometric quantification of immunoblot images (L) showing V5-tagged ACVR1 WT (M) and ACVR1 R206H (N) protein levels in C2C12 cells relative to untreated controls. Statistics, one-way ANOVA with Tukey’s multiple comparisons test; ∗∗∗∗ p < 0.0001. Data are represented as mean ± standard error of the mean ( n = 5–7). NT, non-treated; Lipo, lipofectamine 3000 (a commercially available transfection reagent).

Journal: Molecular Therapy. Nucleic Acids

Article Title: Single-base 2′OMe-modified LNA and MOE gapmers selectively silence ACVR1 R206H in fibrodysplasia ossificans progressiva

doi: 10.1016/j.omtn.2026.102937

Figure Lengend Snippet: Preferential silencing of ACVR1 R206H in FOP patient-derived fibroblasts using LNA and MOE gapmers (A) Sequence alignment showing LNA and MOE gapmer binding sites spanning the ACVR1 c.617G>A mutation (R206H). Mismatches are shown in lowercase; green: ACVR1 WT variant; red: ACVR1 R206H variant. (B) Schematic overview of the experimental timeline: day 2, cell revival; day 0, seeding; day 1, transfection; day 3, RNA/protein harvest. Toxicity assessments were performed at 4, 12, 24, and 48 h post-transfection. (C and D) RT-qPCR analysis of total ACVR1 mRNA levels following treatment with 100 nM (C) or 10 nM (D) gapmers. (E) Representative immunoblots showing total ACVR1 protein levels post-treatment with 100 and 10 nM gapmers. GAPDH served as a loading control. (F and G) Quantification of total ACVR1 protein abundance relative to healthy control cells at 100 nM (F) and 10 nM (G) using densitometric analysis of the immunoblot images (E). (H–K) Allele-specific RT-qPCR quantification of ACVR1 WT (H, J) and ACVR1 R206H (I, K) transcript levels following treatment with 100 nM (H, I) or 10 nM (J, K) gapmers. (L) Representative immunoblots of V5-tagged ACVR1 WT and ACVR1 R206H proteins expressed in C2C12 cells 48 h post-treatment with 10 nM gapmers, with GAPDH as a loading control. (M and N) Densitometric quantification of immunoblot images (L) showing V5-tagged ACVR1 WT (M) and ACVR1 R206H (N) protein levels in C2C12 cells relative to untreated controls. Statistics, one-way ANOVA with Tukey’s multiple comparisons test; ∗∗∗∗ p < 0.0001. Data are represented as mean ± standard error of the mean ( n = 5–7). NT, non-treated; Lipo, lipofectamine 3000 (a commercially available transfection reagent).

Article Snippet: Murine C2C12 myoblasts (American Type Culture Collection, VA, USA) were cultured in DMEM/F-12 medium supplemented with 15% FBS and 0.5% penicillin-streptomycin under standard conditions.

Techniques: Derivative Assay, Sequencing, Binding Assay, Mutagenesis, Variant Assay, Transfection, Quantitative RT-PCR, Western Blot, Control, Quantitative Proteomics

$Single-base 2′OMe modification enhances allele selectivity and suppresses ACVR1 R206H -induced osteogenic differentiation in vitro (A and B) RT-qPCR quantification of ACVR1 WT (A) and ACVR1 R206H (B) transcripts in FOP patient-derived fibroblasts treated with 10 nM LNA16 or MOE3 gapmers, with or without a single 2′OMe modification at the second position of the gap region. (C) Allelic fractions of ACVR1 WT and ACVR1 R206H transcripts post-treatment as calculated from total ACVR1 expression. Green and red bars represent ACVR1 WT and ACVR1 R206H transcript fractions, respectively. (D and E) RT-qPCR quantification of ACVR1 WT (D) and ACVR1 R206H (E) transcripts in C2C12 myoblasts transfected with V5-tagged ACVR1 WT or ACVR1 R206H constructs and treated with 10 nM gapmers for 48 h. (F) Allelic fraction analysis of ACVR1 WT and ACVR1 R206H transcripts in cells from (D and E), similarly as (C). (G) Representative immunoblot showing V5-tagged ACVR1 WT and ACVR1 R206H protein levels in transfected C2C12 cells after 10 nM gapmer treatment. GAPDH served as a loading control. (H and I) Densitometric quantification of ACVR1 WT (H) and ACVR1 R206H (I) protein expression from (G), normalized to GAPDH and expressed relative to the non-treated control. (J) Representative images of alkaline phosphatase (ALP) staining in C2C12 cells expressing V5- ACVR1 R206H or ACVR1 WT , treated with 10 nM gapmers and stimulated with recombinant human activin A (100 ng/mL) for 48 h. (K) Quantification of secreted ALP enzymatic activity in conditioned media collected from cells in (J), normalized to the ACVR1 WT media. (L) Representative images of ARS staining performed 21 days after osteogenic differentiation induction in C2C12 cells transfected with V5- ACVR1 R206H or ACVR1 WT and treated with gapmers. (M) Quantification of ARS staining from (L), normalized to the ACVR1 WT control. Statistics, one-way ANOVA with Tukey’s multiple comparisons test; ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗∗ p < 0.0001. Scale bars, 250 μm. Data are represented as mean ± standard error of the mean ( n = 6–7). NT, non-treated; Lipo, lipofectamine 3000 (a commercially available transfection reagent).$

Journal: Molecular Therapy. Nucleic Acids

Article Title: Single-base 2′OMe-modified LNA and MOE gapmers selectively silence ACVR1 R206H in fibrodysplasia ossificans progressiva

doi: 10.1016/j.omtn.2026.102937

Figure Lengend Snippet: Single-base 2′OMe modification enhances allele selectivity and suppresses ACVR1 R206H -induced osteogenic differentiation in vitro (A and B) RT-qPCR quantification of ACVR1 WT (A) and ACVR1 R206H (B) transcripts in FOP patient-derived fibroblasts treated with 10 nM LNA16 or MOE3 gapmers, with or without a single 2′OMe modification at the second position of the gap region. (C) Allelic fractions of ACVR1 WT and ACVR1 R206H transcripts post-treatment as calculated from total ACVR1 expression. Green and red bars represent ACVR1 WT and ACVR1 R206H transcript fractions, respectively. (D and E) RT-qPCR quantification of ACVR1 WT (D) and ACVR1 R206H (E) transcripts in C2C12 myoblasts transfected with V5-tagged ACVR1 WT or ACVR1 R206H constructs and treated with 10 nM gapmers for 48 h. (F) Allelic fraction analysis of ACVR1 WT and ACVR1 R206H transcripts in cells from (D and E), similarly as (C). (G) Representative immunoblot showing V5-tagged ACVR1 WT and ACVR1 R206H protein levels in transfected C2C12 cells after 10 nM gapmer treatment. GAPDH served as a loading control. (H and I) Densitometric quantification of ACVR1 WT (H) and ACVR1 R206H (I) protein expression from (G), normalized to GAPDH and expressed relative to the non-treated control. (J) Representative images of alkaline phosphatase (ALP) staining in C2C12 cells expressing V5- ACVR1 R206H or ACVR1 WT , treated with 10 nM gapmers and stimulated with recombinant human activin A (100 ng/mL) for 48 h. (K) Quantification of secreted ALP enzymatic activity in conditioned media collected from cells in (J), normalized to the ACVR1 WT media. (L) Representative images of ARS staining performed 21 days after osteogenic differentiation induction in C2C12 cells transfected with V5- ACVR1 R206H or ACVR1 WT and treated with gapmers. (M) Quantification of ARS staining from (L), normalized to the ACVR1 WT control. Statistics, one-way ANOVA with Tukey’s multiple comparisons test; ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗∗ p < 0.0001. Scale bars, 250 μm. Data are represented as mean ± standard error of the mean ( n = 6–7). NT, non-treated; Lipo, lipofectamine 3000 (a commercially available transfection reagent).

Techniques: Modification, In Vitro, Quantitative RT-PCR, Derivative Assay, Expressing, Transfection, Construct, Western Blot, Control, Staining, Recombinant, Activity Assay

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c2c12 myoblasts (ATCC)

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