mouse derived c2c12 myoblasts (ATCC)

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ATCC mouse derived c2c12 myoblasts

Figure 1. Effects of Pueraria montana var. lobata extract (PMLE) on myogenic differentiation in <t>C2C12</t> myoblasts. (A) XTT assay showing no significant effect of PMLE (10, 50, 100 ng/mL) on C2C12 cell viability. Data are mean ± SD. (B) Phase-contrast images of myotube formation after PMLE treatment. Scale bar = 50 µm. (C) qRT-PCR analysis of MyHC, MyoD, and myogenin mRNA levels after PMLE treatment. Data are normalized to GAPDH and shown as fold change vs. control. (D) Western blot analysis of MyHC, MyoD, and myogenin protein levels. GAPDH was used as a loading control. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control.

Mouse Derived C2c12 Myoblasts, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1087 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+derived+c2c12+myoblasts/C2C12%3B+Muscle+Myoblast%3B+Mouse/pm40218975-46-0-3
Average 97 stars, based on 1087 article reviews

mouse derived c2c12 myoblasts - by Bioz Stars, 2026-09

97/100 stars

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1) Product Images from "Dual Action of Pueraria montana var. lobata Extract on Myogenesis and Muscle Atrophy."

Article Title: Dual Action of Pueraria montana var. lobata Extract on Myogenesis and Muscle Atrophy.

Journal: Nutrients

doi: 10.3390/nu17071217

Figure 1. Effects of Pueraria montana var. lobata extract (PMLE) on myogenic differentiation in C2C12 myoblasts. (A) XTT assay showing no significant effect of PMLE (10, 50, 100 ng/mL) on C2C12 cell viability. Data are mean ± SD. (B) Phase-contrast images of myotube formation after PMLE treatment. Scale bar = 50 µm. (C) qRT-PCR analysis of MyHC, MyoD, and myogenin mRNA levels after PMLE treatment. Data are normalized to GAPDH and shown as fold change vs. control. (D) Western blot analysis of MyHC, MyoD, and myogenin protein levels. GAPDH was used as a loading control. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control.

Figure Legend Snippet: Figure 1. Effects of Pueraria montana var. lobata extract (PMLE) on myogenic differentiation in C2C12 myoblasts. (A) XTT assay showing no significant effect of PMLE (10, 50, 100 ng/mL) on C2C12 cell viability. Data are mean ± SD. (B) Phase-contrast images of myotube formation after PMLE treatment. Scale bar = 50 µm. (C) qRT-PCR analysis of MyHC, MyoD, and myogenin mRNA levels after PMLE treatment. Data are normalized to GAPDH and shown as fold change vs. control. (D) Western blot analysis of MyHC, MyoD, and myogenin protein levels. GAPDH was used as a loading control. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control.

Techniques Used: XTT Assay, Quantitative RT-PCR, Control, Western Blot

Figure 2. PMLE enhances mitochondrial biogenesis and protein synthesis signaling pathways in C2C12 myoblasts. (A) qRT-PCR analysis of SIRT1 and PGC-1α mRNA levels after PMLE (10, 50, 100 ng/mL) treatment. Data are normalized to GAPDH and shown as fold change vs. control. (B) Western blot analysis of SIRT1 and PGC-1α protein levels. GAPDH was used as a loading control. (C) Western blot of phosphorylated AMPK (p-AMPK); total AMPK was used as a control. (D) Western blot of p-AKT, p-mTOR, p-p70S6K, and p-4E-BP1; corresponding total proteins were used as loading controls. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control. PMLE, Pueraria montana var. lobata extract.

Figure Legend Snippet: Figure 2. PMLE enhances mitochondrial biogenesis and protein synthesis signaling pathways in C2C12 myoblasts. (A) qRT-PCR analysis of SIRT1 and PGC-1α mRNA levels after PMLE (10, 50, 100 ng/mL) treatment. Data are normalized to GAPDH and shown as fold change vs. control. (B) Western blot analysis of SIRT1 and PGC-1α protein levels. GAPDH was used as a loading control. (C) Western blot of phosphorylated AMPK (p-AMPK); total AMPK was used as a control. (D) Western blot of p-AKT, p-mTOR, p-p70S6K, and p-4E-BP1; corresponding total proteins were used as loading controls. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control. PMLE, Pueraria montana var. lobata extract.

Techniques Used: Protein-Protein interactions, Quantitative RT-PCR, Control, Western Blot

Figure 3. PMLE alleviates dexamethasone (DEX)-induced muscle atrophy and promotes myogenic differentiation in C2C12 myotubes. (A) Immunofluorescence staining of MyHC (green) and nuclei (DAPI, blue) in C2C12 myotubes treated with DEX (100 µM) and/or PMLE (100 ng/mL). The right panel shows the quantification of myotube diameter. (B) qRT-PCR analysis of MyHC, MyoD, and myogenin mRNA levels. Data are normalized to GAPDH and shown as fold change vs. control. (C) Western blot analysis of MyHC, MyoD, and myogenin protein levels. GAPDH was used as a loading control. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01, ### p < 0.001 vs. DEX-treated group. PMLE, Pueraria montana var. lobata extract.

Figure Legend Snippet: Figure 3. PMLE alleviates dexamethasone (DEX)-induced muscle atrophy and promotes myogenic differentiation in C2C12 myotubes. (A) Immunofluorescence staining of MyHC (green) and nuclei (DAPI, blue) in C2C12 myotubes treated with DEX (100 µM) and/or PMLE (100 ng/mL). The right panel shows the quantification of myotube diameter. (B) qRT-PCR analysis of MyHC, MyoD, and myogenin mRNA levels. Data are normalized to GAPDH and shown as fold change vs. control. (C) Western blot analysis of MyHC, MyoD, and myogenin protein levels. GAPDH was used as a loading control. Band intensities are shown as fold change vs. control. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001 vs. control group; # p < 0.05, ## p < 0.01, ### p < 0.001 vs. DEX-treated group. PMLE, Pueraria montana var. lobata extract.

Techniques Used: Immunofluorescence, Staining, Quantitative RT-PCR, Control, Western Blot

Figure 4. PMLE restores mitochondrial biogenesis and protein synthesis signaling pathways in DEX-induced muscle atrophy. (A) qRT-PCR analysis of SIRT1 and PGC-1α mRNA levels in C2C12 myotubes treated with DEX (100 µM) and/or PMLE (100 ng/mL). Data are normalized to GAPDH and shown as fold change vs. control. (B) Western blot of SIRT1 and PGC-1α protein levels. GAPDH was used as a loading control. (C) Western blot of phosphorylated AMPK (p-AMPK); total AMPK was used as a control. (D) Western blot of p-AKT, p-mTOR, p-p70S6K, and p-4E-BP1; total proteins were used as loading controls. Band intensities are presented as fold change vs. control. Statistical significance: * p < 0.05 vs. control group; # p < 0.05, ## p < 0.01, ### p < 0.001 vs. DEX-treated group. PMLE, Pueraria montana var. lobata extract.

Figure Legend Snippet: Figure 4. PMLE restores mitochondrial biogenesis and protein synthesis signaling pathways in DEX-induced muscle atrophy. (A) qRT-PCR analysis of SIRT1 and PGC-1α mRNA levels in C2C12 myotubes treated with DEX (100 µM) and/or PMLE (100 ng/mL). Data are normalized to GAPDH and shown as fold change vs. control. (B) Western blot of SIRT1 and PGC-1α protein levels. GAPDH was used as a loading control. (C) Western blot of phosphorylated AMPK (p-AMPK); total AMPK was used as a control. (D) Western blot of p-AKT, p-mTOR, p-p70S6K, and p-4E-BP1; total proteins were used as loading controls. Band intensities are presented as fold change vs. control. Statistical significance: * p < 0.05 vs. control group; # p < 0.05, ## p < 0.01, ### p < 0.001 vs. DEX-treated group. PMLE, Pueraria montana var. lobata extract.

Techniques Used: Protein-Protein interactions, Quantitative RT-PCR, Control, Western Blot

Cell Culture:

Article Title: The effect of voluntary exercise on light cycle stress-induced metabolic resistance
Article Snippet: .. Mouse-derived C2C12 myoblasts (ATCC, VA, USA) were cultured in a growth medium containing 90% Dulbecco’s modified Eagle’s medium (DMEM; Gibco, NY, USA), 10% fetal bovine serum, and 100 unit/mL penicillin– streptomycin (PS; Gibco) at 37 °C and 5% CO 2 . ..

Article Title: Dual Action of Pueraria montana var. lobata Extract on Myogenesis and Muscle Atrophy.
Article Snippet: Secondary antibodies, including horseradish peroxidase-conjugated anti-mouse and anti-rabbit IgG, were obtained from Enzo Life Sciences (Farmingdale, NY, USA). .. Mouse-derived C2C12 myoblasts (American Type Culture Collection; Manassas, VA, USA; ATCC-CRL 1772) were cultured in a growth medium (GM; DMEM containing 10% heat-inactivated FBS and antibiotics) at 37 ◦C under 5% CO2. ..

Article Title: Modulatory roles of capsaicin on thermogenesis in C2C12 myoblasts and the skeletal muscle of mice.
Article Snippet: Capsaicin, a polyphenol, is known to regulate energy expenditure and thermogenesis in adipocytes and muscles.. However, its role in modulating uncoupling proteins (UCPs) and adenosine triphosphate (ATP)-dependent thermogenesis in muscles remains unclear.. This study investigated the mechanisms underlying the role of capsaicin in modulating the UCPand ATP-dependent thermogenesis in C2C12 myoblasts, as well as the gastrocnemius (GM) and soleus muscles (SM) of mice.

Article Title: Silencing of dopamine receptor D5 inhibits the browning of 3T3-L1 adipocytes and ATP-consuming futile cycles in C2C12 muscle cells.
Article Snippet: Background: As a part of the catecholamines, dopamine receptors (DRs) have not been extensively studied like β3-AR in the thermogenesis process.. The present study investigates the effect of DRD5 in browning events and ATP-consuming futile cycles.. Methods: siRNA technology, qPCR, immunoblot analysis, immunofluorescence, and staining methods were used to investigate the effect of DRD5 on 3T3-L1 and C2C12 cells.

Article Title: The effect of voluntary exercise on light cycle stress-induced metabolic resistance.
Article Snippet: .. Mouse-derived C2C12 myoblasts (ATCC, VA, USA) were cultured in a growth medium containing 90% Dulbecco’s modified Eagle’s medium (DMEM; Gibco, NY, USA), 10% fetal bovine serum, and 100 unit/mL penicillin– streptomycin (PS; Gibco) at 37 °C and 5% CO2. ..

Article Title: Dual Action of Pueraria montana var. lobata Extract on Myogenesis and Muscle Atrophy
Article Snippet: Secondary antibodies, including horseradish peroxidase-conjugated anti-mouse and anti-rabbit IgG, were obtained from Enzo Life Sciences (Farmingdale, NY, USA). .. Mouse-derived C2C12 myoblasts (American Type Culture Collection; Manassas, VA, USA; ATCC-CRL 1772) were cultured in a growth medium (GM; DMEM containing 10% heat-inactivated FBS and antibiotics) at 37 °C under 5% CO 2 . ..

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mouse derived c2c12 myoblasts (ATCC)

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1) Product Images from "Dual Action of Pueraria montana var. lobata Extract on Myogenesis and Muscle Atrophy."

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