MA5-12902

antibody from Invitrogen Antibodies

Targeting: MYOD1 bHLHc1, MYF3, MYOD, PUM

Provider product page for MA5-12902

Western blot

Immunocytochemistry

Other assay

Antibody data

Antibody Data
Antigen structure
References [23]
Comments [0]
Validations
Western blot [1]
Immunocytochemistry [1]
Other assay [14]

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Product number: MA5-12902 - Provider product page
Provider: Invitrogen Antibodies
Product name: MYOD Monoclonal Antibody (5.8A)
Antibody type: Monoclonal
Antigen: Recombinant full-length protein
Description: MA5-12902 targets MyoD1 in IF, IM, and IP applications and shows reactivity with Chicken, Human, mouse, and Rat samples.
Antibody clone number: 5.8A
Concentration: 0.2 mg/mL

MYOD1 protein structure - MA5-12902 shown in red.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Immunoprecipitation of MyoD1 using MyoD1 Monoclonal Antibody (Product # MA5-12902) on Native Human SW80 Cells.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 5--figure supplement 1. HES3 overexpression inhibits the myogenic differentiation kinetic in mouse muscle myoblasts. ( A ) C2C12 cells were transfected with control or CMV- HES3 , allowed to become confluent and begin fusion, and then whole cell lysate harvested four days post plating. ( B ) Western blots to detect Myosin, MyoD, MYC-HES3, and Tubulin protein expression levels. ( C ) Entire membranes for the cropped images shown in panel B.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 5--figure supplement 2. HES3 does not alter MyoD expression during fusion initiation but inhibits MyoD during terminal differentiation. ( A ) C2C12 cells were transfected with CMV-Empty or CMV-HES3, allowed to become confluent, and then whole cell lysate harvested 4 days post plating. Remaining C2C12 conditions were changed to differentiation media, fused, and whole cell lysate was harvested at 9 days post plating. ( B ) The kinetic of MyoD protein expression was evaluated between the beginning and end of myogenic differentiation. Shown are representative Western blots for MyoD, MYC-HES3, and tubulin for three biological replicates from day 3 and day 9 of fusion. HES3 is presented on two independent blots (demarcated by a black line) between days 3 and 9. ( C ) Quantification of MyoD expression levels by densitometry. MyoD was normalized to the tubulin loading control. Plotted is the ratio of MyoD/Tubulin for each sample with n = 3 biological replicates per group +- SEM. Significance was assessed with a two-tailed Student's t-test.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 4. Representative results of immunofluorescence staining of satellite cells on a freshly isolated myofiber and on a myofiber after cultured in floating condition for 72 h. Pax7 is expressed in the nuclei of quiescent satellite cells (A, white arrow) while MyoD is expressed in the nuclei of activated satellite cells (D, yellow arrowhead). All myonuclei present were revealed by counterstaining with DAPI (B and E). The merged fluorescence image of both Pax7-staining and DAPI-staining of a quiescent satellite cell (C, white arrow). The merged fluorescence image of both MyoD-staining and DAPI-staining of an activated satellite cell (F, yellow arrow). The scale bar represents 2000 mum.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Fig 5 Co-localization of the R&D BAI1 mAb with antibodies to Noggin and MyoD in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R&D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 muM.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Fig 2 Myo/Nog cells contain ink in human tattooed skin. Tissue sections of tattooed skin were double labeled with the G8 mAb and antibodies to Noggin (Nog) (A-D), MyoD (F-I) or alpha-SMA (K-N). The colors of the secondary antibodies are indicated in the photographs. Nuclei were stained with Hoechst dye (blue). Images were produced with the epifluorescence (A-E, J and O) and confocal microscopes (F-I and K-N) with 60x lenses. Overlap of green and red fluorescence appears yellow in merged images (C, D, H, I, M and N). Fluorescent photomicrographs were merged with the corresponding DIC image to visualize the ink (black in D, I and N). Some double labeled cells appeared to contain ink (arrows in D, I and N). All ink laden G8+ cells were alpha-SMA+ (N). Smooth muscle cells of blood vessels also contained alpha-SMA (K). Minimal to no background fluorescence was visible after staining with the anti-goat (E), anti-IgM and anti-IgG (I), and anti-rabbit (O) secondary antibodies only. Bar = 28 muM in E and 5.6 muM in A-D and G-O.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 1: FOXP1 and MyoD are coordinately expressed and interact physically in vivo . A, B. FOXP1 and MyoD expression peaks at ~3 days following serum withdrawal-mediated differentiation in C2C12 myocytes and or 5-azacytidine-mediated differentiation in 10T1/2 fibroblasts. SDS-PAGE fractionation was followed by anti-MyoD Ab or anti-FOXP1 Ab Western blotting. C. FOXP1 and MyoD heterodimerize in differentiated C2C12 myoblasts. Standard co-immunoprecipitation (Co-IP)/Western blotting was performed 3 days following serum withdrawal. Nuclear lysates were immunoprecipitated with anti-FOXPI Ab, fractionated on SDS gels and then blotted with anti-MyoD Ab. IP, immunoprecipitation; WB, Western blotting; Loading controls (CTRL) include 1% input lanes, 1% IP'd lanes, Ig-only, and beta- tubulin loading controls. Molecular weights are indicated on the right.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 5: FOXP1 retards MyoD-mediated myoblastic differentiation. A. C2C12 myocytes were infected with lentivirus Foxp1-EF1a-TetRGFP-Bsd ), cultured for several generations (black arrow). At 18 hr following initiation of differentiation (green arrow), Tet on FOXP1 overexpression (OE) was initiated by addition of 1 µg/mL doxycycline (dox) as detailed in Materials and Methods . OE kinetics of GFP-illuminated C2C12 cells were measured through day 6. Mock transduced control C2C12 (CTRL) myocytes converted to myoblasts by day 4, whereas FOXP1 OE myoblast conversion was significantly retarded as judged by morphology and GFP fluorescence (green). B. Quantification of the data of (A) using epifluorescence microscopy. Shown is the mean of 5 independent measurements (p

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Fig. 1. A reprogrammable system to study lineage conversion into myogenic cells. ( A ) Schematic of experimental design denoting the conversion of Thy1 + Pax7-nGFP Rep-MEFs into multinucleated myotubes solely by MyoD overexpression or iMPCs by MyoD+F/R/C treatment. ( B ) Representative bright-field images of Thy1 + Rep-MEFs subjected to either MyoD or MyoD+F/R/C treatment for the indicated days. Scale bars, 400 mum. ( C ) Bar graphs based on flow cytometry analysis showing the percentage of EdU + cells in Thy1 + Rep-MEFs subjected to either the MyoD or MyoD+F/R/C condition for the indicated days. ( D ) qRT-PCR for the indicated myogenic genes at day 10. Data are shown as means +- SD. N = 3 cell lines per group. Statistical significance was determined by a two-tailed unpaired t test (* P < 0.05; ** P < 0.01; **** P < 0.0001; n.s., nonsignificant). ( E ) Representative images of a stable Pax7-nGFP iMPC clone at passage 1. Scale bar, 100 mum. ( F ) Flow cytometry analysis of a Pax7-nGFP iMPC clone at P1. ( G ) Representative immunofluorescence images of iMPCs immunostained for Mki67 and Pax7. Nuclei were counterstained with DAPI. Scale bar, 100 mum. ( H ) Quantification of (G). Three different images were quantified from the respective iMPC clone. ( I ) Representative immunofluorescence images of Pax7-nGFP iMPCs immunostained for MyoD and MyHC. Nuclei were counterstained with DAPI. White arrowheads point to mononucleated Pax7-nGFP + cells. Scale bar, 100 mum. ( J ) Quantificatio

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Fig 5 Co-localization of antibodies to G8 and MyoD in human RMS and Wilms tumor tissue sections. Sections of human ARMS from soft tissue, ERMS from the retroperitoneum, spindle cell RMS (SCRMS) from the testis, pleomorphic RMS (PRMS) from striated muscle and Wilms (kidney) tumors were double labeled with antibodies to G8 (red) and MyoD (green). Nuclei were stained with Hoechst dye (blue). Overlap of red and green appears yellow in merged images. RMS and Wilms tumors sections contain subpopulations of G8+/MyoD- cells (red arrows), G8-/MyoD+ cells (green arrows) and G8+/MyoD+ cells (white arrows). Bar = 9 muM.