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Myod c 20

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MyoD (C-20) is a primary antibody specific for the MyoD protein. MyoD is a transcription factor that plays a crucial role in regulating muscle cell differentiation and development.

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Lab products found in correlation

Protein assay, by Bio-Rad (2 mentions) Celllytic nuclear extraction kit, by Merck Group (2 mentions) Myogenin, by Santa Cruz Biotechnology (1 mentions) Donkey serum, by Cedarlane (1 mentions) Mouse anti biotin, by Jackson ImmunoResearch (1 mentions) C ebpβ, by Abcam (1 mentions) Alexa flour 647, by Jackson ImmunoResearch (1 mentions) Cyanine3 (cy3), by Jackson ImmunoResearch (1 mentions) Alexa 488, by Jackson ImmunoResearch (1 mentions) Goat serum, by Cedarlane (1 mentions) Alexa fluor 594, by Thermo Fisher Scientific (1 mentions) Anti fade mounting media, by Vector Laboratories (1 mentions) Serum free block solution, by Agilent Technologies (1 mentions) Pdgf bb, by R&D Systems (1 mentions) Tgf β1, by R&D Systems (1 mentions) Laminin, by Abcam (1 mentions) Myogenin, by Developmental Studies Hybridoma Bank (1 mentions) Gfp fl, by Santa Cruz Biotechnology (1 mentions)

5 protocols using myod c 20

1

Immunofluorescence Staining of Myogenic Cells

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Myofibers were fixed in 4% paraformaldehyde (PFA) in PBS and 1% glycine and blocked in PBS containing 0.2% Triton X-100 (BioShop), 2% BSA, 5% goat serum (Cedarlane), and 1% azide. Myoblasts were fixed in 2% PFA in PBS and blocked in PBS containing 0.3% Triton X-100 and 10% goat serum. Cryosections were thawed at room temperature, fixed in 4% PFA, and processed for antigen retrieval in citrate buffer at 95 °C for 20 min. The sections were permeabilized with PBS containing 0.5% Triton X-100 and blocked in PBS containing 0.1% Triton X-100 and 5% donkey serum (Cedarlane) prior to incubation with primary antibody overnight at 4 °C. The cells were washed with PBS and incubated in biotin anti-mouse (when indicated) or secondary antibodies conjugated to a fluorescent dye (Cy3, Alexa 488, or Alexa Flour 647; all from Jackson ImmunoResearch). Nuclei were counterstained with DAPI (0.5 μg/ml). The primary antibodies used were as follows: Pax7-c (DSHB), MYH (H-300; Santa Cruz), MyoD (C-20; Santa Cruz), myogenin (M-225; Santa Cruz), C/EBPβ (E299; Abcam), and laminin (AL-4; Millipore).
Lala-Tabbert N., AlSudais H., Marchildon F., Fu D, & Wiper-Bergeron N. (2016). CCAAT/enhancer binding protein β is required for satellite cell self-renewal. Skeletal Muscle, 6, 40.
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2

Nuclear Extraction and DNA-Protein Binding Assays

Cited 1 time
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Nuclear extracts were prepared from the various cell lines using the CellLytic NuCLEAR extraction kit (Sigma-Aldrich, St. Louis, MO). Protein concentration was measured with a Bio-Rad protein assay (Hercules, CA), and samples were stored at −70°C until use. Double-stranded DNA oligonucleotide probes corresponding to the predicted TF binding sites of KIR ProI region were synthesized (Figures 2, 3, 5). Labeling and DNA-protein binding reactions were performed as previous described9 (link). For antibody supershift experiments, nuclear extracts were incubated with 2 µL of antibody for 1 h on ice before the addition of 32P-labeled DNA probe. After the addition of labeled DNA probe, the binding reaction was incubated for an additional 20 min at room temperature. The antibodies used were cFos (6-2H-2F), FosB (102), cJun (H-79), JunB (C-11), JunD (329), Fra-2 (Q-20), ATF-1 (FI-1), Ets-1 (C-4), Elf-1 (C-20), Oct-1 (E-8, C-21 and 12F11), Oct-3/4 (C-10), Oct-2 (C-20), CREB-1 (24H4B), C/EBPα (D-5), C/EBPβ (H-7), C/EBPγ (H-50), SP-1 (E-3), IRF-1 (C-20), IRF-3 (SL-12), ICSBP (C-19), PU.1 (A-7), E4BP4 (B-1), and MyoD (C-20) from Santa Cruz Biotechnology, Inc. (Dallas, TX, USA) at gel shift grade (200 µg/0.1µl)
Li H., Wright P.W., McCullen M, & Anderson S.K. (2015). Characterization of KIR intermediate promoters reveals four promoter types associated with distinct expression patterns of KIR subtypes. Genes and immunity, 17(1), 66-74.
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3

Smooth Muscle Differentiation of hUSCs

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hUSCs were plated at 2000 cells/cm2 in smooth muscle differentiation media containing equal amounts of high-glucose DMEM and embryonic fibroblast medium (EFM) with 10% FBS, 2.5 ng/mL of transforming growth factor beta1 (TGF-β1), and 5 ng/mL of platelet-derived growth factor BB (PDGF-BB) (R&D Systems, Minneapolis, MN). Cell morphology was recorded before and after growth factor additions for up to 14 days. The slides were fixed with freshly prepared 4% paraformaldehyde for 20 min followed by permeabilization with 0.1% Triton-X100 in PBS for 10 min and blocked with serum-free block solution (Dako, Denmark) for 15 min. Lineage-specific primary antibodies, rabbit polyclonal antibodies to desmin (abcam, Cambridge, MA; catalog number ab15200) and MyoD (C-20, Santa Cruz Biotechnology, Inc., Dallas, TX; catalog number sc-304), were incubated at 4°C overnight followed by secondary antibody conjugated to Alexa Fluor 594 (Life Technologies, Grand Island, NY; catalog number A11072) for 30 min in the dark. The slides were mounted using anti-fade mounting media (Vector Laboratories, Inc., Burlingame, CA) containing propidium iodide (PI) and images were captured using a Leica upright microscope (DM 4000B, Wetzlar, Germany).
Pei M., Li J., Zhang Y., Liu G., Wei L, & Zhang Y. (2014). Expansion on matrix deposited by nonchondrogenic urine stem cells strengthens repeated passage bone marrow stromal cells’ chondrogenic capacity. Cell and tissue research, 356(2), 391-403.
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4

Immunohistochemistry for Skeletal Muscle

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Mouse anti-human nuclei (1:50) (Millipore MAB1281), Pax7 (1:500), Pax3 (1:500), Myogenin (1:500) (Developmental Studies Hybridoma Bank), Laminin (C-20) (1:200) (Sigma), Laminin (1:400) (Abcam), MyoD (C-20) (1:100), Desmin (RD301) (1:50), and GFP (FL) (1:50) (Santa Cruz).
Wang Z., Cheung D., Zhou Y., Han C., Fennelly C., Criswell T, & Soker S. (2014). An In Vitro Culture System That Supports Robust Expansion and Maintenance of In Vivo Engraftment Capabilities for Myogenic Progenitor Cells from Adult Mice. BioResearch Open Access, 3(3), 79-87.
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5

Nuclear Extraction and DNA-Protein Binding Assays

Cited 1 time
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Nuclear extracts were prepared from the various cell lines using the CellLytic NuCLEAR extraction kit (Sigma-Aldrich, St. Louis, MO). Protein concentration was measured with a Bio-Rad protein assay (Hercules, CA), and samples were stored at −70°C until use. Double-stranded DNA oligonucleotide probes corresponding to the predicted TF binding sites of KIR ProI region were synthesized (Figures 2, 3, 5). Labeling and DNA-protein binding reactions were performed as previous described9 (link). For antibody supershift experiments, nuclear extracts were incubated with 2 µL of antibody for 1 h on ice before the addition of 32P-labeled DNA probe. After the addition of labeled DNA probe, the binding reaction was incubated for an additional 20 min at room temperature. The antibodies used were cFos (6-2H-2F), FosB (102), cJun (H-79), JunB (C-11), JunD (329), Fra-2 (Q-20), ATF-1 (FI-1), Ets-1 (C-4), Elf-1 (C-20), Oct-1 (E-8, C-21 and 12F11), Oct-3/4 (C-10), Oct-2 (C-20), CREB-1 (24H4B), C/EBPα (D-5), C/EBPβ (H-7), C/EBPγ (H-50), SP-1 (E-3), IRF-1 (C-20), IRF-3 (SL-12), ICSBP (C-19), PU.1 (A-7), E4BP4 (B-1), and MyoD (C-20) from Santa Cruz Biotechnology, Inc. (Dallas, TX, USA) at gel shift grade (200 µg/0.1µl)
Li H., Wright P.W., McCullen M, & Anderson S.K. (2015). Characterization of KIR intermediate promoters reveals four promoter types associated with distinct expression patterns of KIR subtypes. Genes and immunity, 17(1), 66-74.
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