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Myosin heavy chain

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Myosin heavy chain is a structural protein found in muscle cells. It is a key component of the muscle contractile apparatus, playing a crucial role in muscle contraction and movement.

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Lab products found in correlation

Dulbecco s modified eagle medium, by Thermo Fisher Scientific (1 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions) Live dead viability cytotoxicity kit, by Promega (1 mentions) C2c12 mouse myoblast cells, by American Type Culture Collection (1 mentions) Mtt cell proliferation assay kit, by Promega (1 mentions) Myogenin, by Abcam (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions) Biotinylated secondary antibody, by Vector Laboratories (1 mentions) α smooth muscle actin, by Agilent Technologies (1 mentions) 3 3 diaminobenzidine (dab), by Vector Laboratories (1 mentions) Von willebrand factor, by Agilent Technologies (1 mentions) Gill s hematoxylin, by Vector Laboratories (1 mentions)

Spelling variants of this product

Anti-myosin heavy chain (7 citations) Anti-myosin heavy chain antibody (2 citations) Anti-fast myosin skeletal heavy chain (2 citations) Mouse monoclonal [1C10] to smooth muscle Myosin heavy chain I (2 citations) Smooth Muscle Myosin Heavy Chain (SMMHC, (2 citations) Anti-α-myosin heavy chain (α-MHC, (2 citations) β-myosin heavy chain (β-MHC; (2 citations) Smooth muscle Myosin heavy chain 11(SMMHC) (1 citations)

5 protocols using myosin heavy chain

1

Peptide-Mediated Myoblast Proliferation

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Two tetrameric self-assembling peptides CH-01 and CH-02 were custom-synthesized in our Laboratory for Nanomedicine. Mouse myoblast cells (C2C12) were obtained from ATCC, USA. The following materials were ordered from Gibco, USA: Dulbecco’s modified eagle medium (DMEM), fetal bovine serum (FBS), heat-inactivated horse serum, Dulbecco’s phosphate-buffered saline (PBS) solution, and penicillin-streptomycin (P/S) antibiotics. An 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) cell proliferation assay kit and a LIVE/DEAD Viability/Cytotoxicity kit were purchased from Promega, USA. Immunostaining antibody myosin heavy chain (MHC) was purchased from Abcam. Cell culture flasks and 96-well plates were ordered from Corning, USA.
Arab W., Kahin K., Khan Z, & Hauser C.A. (2019). Exploring nanofibrous self-assembling peptide hydrogels using mouse myoblast cells for three-dimensional bioprinting and tissue engineering applications. International Journal of Bioprinting, 5(2), 198.
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2

Myogenic Differentiation of Rat L6 Cells

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Rat myoblast L6 cells were used in this experiment and were divided into 4 groups: (I) control; (II) induction; (III) Li-ESWT; and (IV) induction + Li-ESW. Control and Induction groups were cells cultured in DMEM containing 15% FBS and 2% horse serum, respectively. Li-ESW groups were cells treated with Li-ESW at 0.03 mJ/mm2 for 200 shocks. All groups were stained for Myosin heavy chain (MHC) (1:500, Abcam Inc., MA, USA) and Myogenin (1:500, Abcam Inc., MA, USA), followed by microscopy and photography at 7 days.
Wu A.K., Zhang X., Wang J., Ning H., Zaid U., Villalta J.D., Wang G., Banie L., Lin G, & Lue T.F. (2018). Treatment of stress urinary incontinence with low-intensity extracorporeal shock wave therapy in a vaginal balloon dilation induced rat model. Translational Andrology and Urology, 7(Suppl 1), S7-S16.
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3

Western Blot Analysis of Myogenic Markers

Cited 3 times
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Stably transduced cells were grown to 80% confluency, harvested, and total cell extracts made, as previously described [21 (link)–23 (link), 36 (link)]. Equal amounts of total cell lysates (12μg) were separated by 8% SDS-PAGE and analyzed by Western blot analysis using antibodies specific for Pax3, as previously described [21 (link), 22 (link)], or MyoD (GenScript, Piscataway, NJ), Myogenein (Abcam, Cambridge, MA), Myosin heavy chain (Abcam), or GAPDH (Cell Signaling, Danvers, MA), according to manufacturers’ specifications.
Loupe J.M., Miller P.J., Crabtree J.S., Zabaleta J, & Hollenbach A.D. (2017). Acquisition of an oncogenic fusion protein is sufficient to globally alter the landscape of miRNA expression to inhibit myogenic differentiation. Oncotarget, 8(50), 87054-87072.
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4

Histological Analysis of Explanted TEVG

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Explanted TEVG samples were fixed in 10% formalin for 24 hours
at 4 °C, and then embedded in paraffin. For standard histology, tissue
sections were stained with hematoxylin and eosin, Masson trichrome, picrosirius
red, Hart, and von Kossa stains. For immunohistochemistry, tissue sections were
deparaffinized, rehydrated, and blocked for endogenous peroxidase activity and
nonspecific staining. The primary antibodies used included von Willebrand factor
(1:2000; Dako, Carpinteria, Calif), α-smooth muscle
actin (1:500; Dako), myosin heavy chain (1:500; Abcam, Cambridge, Mass), and
CD68 (1:200, Abcam). Antibody binding was detected using biotinylated secondary
antibodies (Vector Laboratories, Burlingame, Calif), followed by incubation with
streptavidinated horseradish peroxidase (Vector Laboratories). Development was
performed by chromogenic reaction with 3,3-diaminobenzidine (Vector
Laboratories). Nuclei were counterstained with Gill’s hematoxylin
(Vector Laboratories).
Fukunishi T., Best C.A., Sugiura T., Opfermann J., Ong C.S., Shinoka T., Breuer C.K., Krieger A., Johnson J, & Hibino N. (2016). Preclinical study of patient-specific cell-free nanofiber tissue-engineered vascular grafts using 3-dimensional printing in a sheep model. The Journal of thoracic and cardiovascular surgery, 153(4), 924-932.
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5

Quantifying Myosin Degradation in Myocytes

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Immunohistochemical analyses were performed by confocal microscopy using myosin heavy chain (Abcam, Cambridge, MA, USA) primary antibody followed by Cy3 (Red, Chemicon, Temecula, CA, USA)-conjugated secondary antibody. Nuclei were counterstained using DAPI. Myosin degradation was quantified as the cytoplasmic myosin (MHC) area divided by the nuclear area. The relative expression levels of MHC were normalized to the control level. For each analysis, at least five fields were selected at random to observe >30 myocytes.
Tsai F.C., Chang G.J., Lai Y.J., Chang S.H., Chen W.J, & Yeh Y.H. (2020). Ubiquitin Pathway Is Associated with Worsening Left Ventricle Function after Mitral Valve Repair: A Global Gene Expression Study. International Journal of Molecular Sciences, 21(14), 5073.
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