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Mouse Anti-MYOD1 (AA 180-189) Recombinant Antibody (CBFYM-3000) (CBMAB-M3195-FY)

This product is mouse antibody that recognizes MYOD1. The antibody CBFYM-3000 can be used for immunoassay techniques such as: WB, IP, IHC, ICC, IF.
See all MYOD1 antibodies

Summary

Host Animal
Mouse
Specificity
Cat, Human, Mouse, Rat
Clone
CBFYM-3000
Antibody Isotype
IgG1, k
Application
WB, IP, IHC, ICC, IF

Basic Information

Immunogen
Recognizes mouse MyoD. Species Crossreactivity: human, rat, and feline
Specificity
Cat, Human, Mouse, Rat
Antibody Isotype
IgG1, k
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.5% BSA
Preservative
0.05% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 180-189

Target

Full Name
Myogenic Differentiation 1
Introduction
This gene encodes a nuclear protein that belongs to the basic helix-loop-helix family of transcription factors and the myogenic factors subfamily. It regulates muscle cell differentiation by inducing cell cycle arrest, a prerequisite for myogenic initiation. The protein is also involved in muscle regeneration. It activates its own transcription which may stabilize commitment to myogenesis.
Entrez Gene ID
Human4654
Mouse17927
Rat337868
Cat101097667
UniProt ID
HumanP15172
MouseP10085
RatQ02346
CatM3W380
Alternative Names
Myogenic Differentiation 1; Myogenic Factor 3; Class C Basic Helix-Loop-Helix Protein 1; Myoblast Determination Protein 1; BHLHc1; Myf-3; MYF3; MYOD; PUM
Function
Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity).
Biological Process
Cellular response to estradiol stimulus Source: UniProtKB
Cellular response to glucocorticoid stimulus Source: Ensembl
Cellular response to oxygen levels Source: Ensembl
Cellular response to starvation Source: Ensembl
Cellular response to tumor necrosis factor Source: Ensembl
Histone H3 acetylation Source: UniProtKB
Histone H4 acetylation Source: UniProtKB
Muscle cell fate commitment Source: BHF-UCL
Muscle organ development Source: ProtInc
Myoblast fate determination Source: Ensembl
Myoblast fusion Source: Ensembl
Myotube cell development Source: BHF-UCL
Myotube differentiation involved in skeletal muscle regeneration Source: Ensembl
Negative regulation of chromatin binding Source: Ensembl
Negative regulation of myoblast proliferation Source: Ensembl
Positive regulation of binding Source: Ensembl
Positive regulation of muscle cell differentiation Source: BHF-UCL
Positive regulation of myoblast differentiation Source: GO_Central
Positive regulation of myoblast fusion Source: BHF-UCL
Positive regulation of skeletal muscle fiber development Source: GO_Central
Positive regulation of skeletal muscle tissue regeneration Source: Ensembl
Positive regulation of snRNA transcription by RNA polymerase II Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: NTNU_SB
Protein phosphorylation Source: ProtInc
Regulation of alternative mRNA splicing, via spliceosome Source: Ensembl
Regulation of RNA splicing Source: BHF-UCL
Regulation of transcription by RNA polymerase II Source: GO_Central
Skeletal muscle cell differentiation Source: GO_Central
Skeletal muscle fiber adaptation Source: Ensembl
Skeletal muscle fiber development Source: Ensembl
Skeletal muscle tissue development Source: ProtInc
Cellular Location
Nucleus
Involvement in disease
Myopathy, congenital, with diaphragmatic defects, respiratory insufficiency, and dysmorphic facies (MYODRIF):
An autosomal recessive muscular disorder characterized by hypotonia and respiratory insufficiency apparent soon after birth, high diaphragmatic dome on imaging, poor overall growth, pectus excavatum, dysmorphic facies, and renal anomalies in some affected individuals. Additional variable features include delayed motor development, mildly decreased endurance, distal arthrogryposis, and lung hypoplasia resulting in early death.
PTM
Phosphorylated by CDK9. This phosphorylation promotes its function in muscle differentiation.
Acetylated by a complex containing EP300 and PCAF. The acetylation is essential to activate target genes. Conversely, its deacetylation by SIRT1 inhibits its function (By similarity).
Ubiquitinated on the N-terminus; which is required for proteasomal degradation.
Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity.

Gellhaus, B., Böker, K. O., Gsaenger, M., Rodenwaldt, E., Hüser, M. A., Schilling, A. F., & Saul, D. (2023). Foxo3 knockdown mediates decline of Myod1 and Myog reducing myoblast conversion to myotubes. Cells, 12(17), 2167.

Tuohy, J. L., Byer, B. J., Royer, S., Keller, C., Nagai-Singer, M. A., Regan, D. P., & Seguin, B. (2021). Evaluation of myogenin and MyoD1 as immunohistochemical markers of canine rhabdomyosarcoma. Veterinary pathology, 58(3), 516-526.

Jeong, J., Choi, K. H., Kim, S. H., Lee, D. K., Oh, J. N., Lee, M., ... & Lee, C. K. (2021). Combination of cell signaling molecules can facilitate MYOD1-mediated myogenic transdifferentiation of pig fibroblasts. Journal of Animal Science and Biotechnology, 12(1), 1-13.

Rovito, D., Rerra, A. I., Ueberschlag-Pitiot, V., Joshi, S., Karasu, N., Dacleu-Siewe, V., ... & Metzger, D. (2021). Myod1 and GR coordinate myofiber-specific transcriptional enhancers. Nucleic acids research, 49(8), 4472-4492.

Ahmed, A. A., Habeebu, S., Farooqi, M. S., Gamis, A. S., Gonzalez, E., Flatt, T., ... & Tsokos, M. G. (2021). MYOD1 as a prognostic indicator in rhabdomyosarcoma. Pediatric blood & cancer, 68(9), e29085.

Lee, Q. Y., Mall, M., Chanda, S., Zhou, B., Sharma, K. S., Schaukowitch, K., ... & Wernig, M. (2020). Pro-neuronal activity of Myod1 due to promiscuous binding to neuronal genes. Nature cell biology, 22(4), 401-411.

Wu, F., Qin, Y., Jiang, Q., Zhang, J., Li, F., Li, Q., ... & Huang, C. (2020). MyoD1 suppresses cell migration and invasion by inhibiting FUT4 transcription in human gastric cancer cells. Cancer Gene Therapy, 27(10-11), 773-784.

Agaram, N. P., LaQuaglia, M. P., Alaggio, R., Zhang, L., Fujisawa, Y., Ladanyi, M., ... & Antonescu, C. R. (2019). MYOD1-mutant spindle cell and sclerosing rhabdomyosarcoma: an aggressive subtype irrespective of age. A reappraisal for molecular classification and risk stratification. Modern pathology, 32(1), 27-36.

Hodge, B. A., Zhang, X., Gutierrez-Monreal, M. A., Cao, Y., Hammers, D. W., Yao, Z., ... & Esser, K. A. (2019). MYOD1 functions as a clock amplifier as well as a critical co-factor for downstream circadian gene expression in muscle. Elife, 8, e43017.

Takizawa, H., Hara, Y., Mizobe, Y., Ohno, T., Suzuki, S., Inoue, K., ... & Aoki, Y. (2019). Modelling Duchenne muscular dystrophy in MYOD1-converted urine-derived cells treated with 3-deazaneplanocin A hydrochloride. Scientific Reports, 9(1), 3807.

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For research use only. Not intended for any clinical use.

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