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90
StressMarq mouse anti myomesin antibody
Fig. 2. Inhibition of heat shock protein 90 (HSP90) activity slows the myosin replacement rate in myofibrils. A–L: sarcomere structures were not disrupted by geldanamycin (GM) treatment. DMSO (A–C and G–I) or 5 g/ml GM (D–F and J–L)-treated cells were stained with <t>indicated</t> <t>antibodies.</t> C, F, I, and L are merged images of A and B, D and E, G and H, and J and K. Arrowheads depict <t>myomesin-positive</t> M-lines in the A-bands in A–F. All images were taken with a confocal microscope. Scale bars 10 m. M–O: relative fluo- rescence intensity after bleaching of green fluorescent protein-tagged myosin heavy chain 3 (GFP-MYH3) was measured in myotubes treated with DMSO or GM. Fluorescence signals were measured at indicated time points (M). Mobile fractions (%) of GFP-MYH3 were 47.0 5.9 in DMSO and 9.6 1.2 in GM (N). Half- lives (hours) of GFP-MYH3 were 6.7 1.2 in DMSO and 3.4 1.0 in GM (O). Values represent the mean SE. *P 0.05, significant difference compared with DMSO control. DMSO control myotubes, n 7; GM-treated myotubes, n 4.
Mouse Anti Myomesin Antibody, supplied by StressMarq, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Fig. 2. Inhibition of heat shock protein 90 (HSP90) activity slows the myosin replacement rate in myofibrils. A–L: sarcomere structures were not disrupted by geldanamycin (GM) treatment. DMSO (A–C and G–I) or 5 g/ml GM (D–F and J–L)-treated cells were stained with indicated antibodies. C, F, I, and L are merged images of A and B, D and E, G and H, and J and K. Arrowheads depict myomesin-positive M-lines in the A-bands in A–F. All images were taken with a confocal microscope. Scale bars 10 m. M–O: relative fluo- rescence intensity after bleaching of green fluorescent protein-tagged myosin heavy chain 3 (GFP-MYH3) was measured in myotubes treated with DMSO or GM. Fluorescence signals were measured at indicated time points (M). Mobile fractions (%) of GFP-MYH3 were 47.0 5.9 in DMSO and 9.6 1.2 in GM (N). Half- lives (hours) of GFP-MYH3 were 6.7 1.2 in DMSO and 3.4 1.0 in GM (O). Values represent the mean SE. *P 0.05, significant difference compared with DMSO control. DMSO control myotubes, n 7; GM-treated myotubes, n 4.

Journal: American journal of physiology. Cell physiology

Article Title: HSP90 modulates the myosin replacement rate in myofibrils.

doi: 10.1152/ajpcell.00245.2017

Figure Lengend Snippet: Fig. 2. Inhibition of heat shock protein 90 (HSP90) activity slows the myosin replacement rate in myofibrils. A–L: sarcomere structures were not disrupted by geldanamycin (GM) treatment. DMSO (A–C and G–I) or 5 g/ml GM (D–F and J–L)-treated cells were stained with indicated antibodies. C, F, I, and L are merged images of A and B, D and E, G and H, and J and K. Arrowheads depict myomesin-positive M-lines in the A-bands in A–F. All images were taken with a confocal microscope. Scale bars 10 m. M–O: relative fluo- rescence intensity after bleaching of green fluorescent protein-tagged myosin heavy chain 3 (GFP-MYH3) was measured in myotubes treated with DMSO or GM. Fluorescence signals were measured at indicated time points (M). Mobile fractions (%) of GFP-MYH3 were 47.0 5.9 in DMSO and 9.6 1.2 in GM (N). Half- lives (hours) of GFP-MYH3 were 6.7 1.2 in DMSO and 3.4 1.0 in GM (O). Values represent the mean SE. *P 0.05, significant difference compared with DMSO control. DMSO control myotubes, n 7; GM-treated myotubes, n 4.

Article Snippet: The antibodies used in this study were mouse anti-myomesin antibody (1:10 dilution; clone B4; Developmental Studies Hybridoma Bank, University of Iowa, Iowa City, IA) (19), mouse anti-HSP90 antibody (1:400 dilution; clone D7 ; StressMarq Biosciences), and rabbit polyclonal anti-MYH antibody (1:500 dilution; kindly gifted by the late Prof. Howard Holtzer, University of Pennsylvania, Philadelphia).

Techniques: Inhibition, Activity Assay, Staining, Microscopy, Fluorescence, Control