N3.36

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$40.00
SKU: N3.36
View product citations for antibody N3.36 on CiteAb

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Available: 153

DSHB Data Sheet

Catalog Fields

Antigen: Myosin heavy chain (human neonatal and adult fast fibers)
Hybridoma Cells Available: Yes
Antigen Species: Human
Depositor: Blau, H.M.
Isotype: MIgM
Antigen Sequence:
Host Species: mouse
Depositors Institution: Baxter Lab for Stem Cell Biology, Stanford University
Positive Tested Species Reactivity: Bovine, Human, Rodent
Depositors Notes: Fusion: 1983. Recognizes neonatal and adult fast fibers.
Antigen Molecular Weight: 220kDa
Human Protein Atlas:
Predicted Species Reactivity:  
Gene: MYH8
Immunogen: partially purified myosin (pyrophosphate extracted) from human neonatal (5 days old) skeletal muscle
Alternate Gene Names: DA7; MyHC-pn; gtMHC-F; MyHC-peri
Alternate Antibody Name:
Clonality: Monoclonal
Alternate Antigen Name:
Epitope Mapped:
Myeloma Strain: SP2/2
Epitope Location or Sequence:
Uniprot ID: P13535 
Immunogen Sequence:
Entrez Gene ID: 4626 
Additional Characterization:
Antibody Registry ID: AB_528380 
Additional Information: This antibody may recognize more than one myosin isoform depending on the tissue, developmental stage, or species. The gene, Uniprot ID and gene ID associated with this mAb are not exclusive.
Recommended Applications: ELISA, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot
These hybridomas were created by your colleagues. Please acknowledge the hybridoma contributor and the Developmental Studies Hybridoma Bank (DSHB) in the Materials and Methods of your publications. Please email the citation to us.
For your Materials & Methods section:
N3.36 was deposited to the DSHB by Blau, H.M. (DSHB Hybridoma Product N3.36)
Storage and Handling Recommendations
Although many cell products are maintained at 4°C for years without loss of activity, shelf-life at 4°C is highly variable. To ensure retention of antibody activity, we recommend aliquotting the product into two parts: 1) a volume of antibody stored at 4°C to be used within two weeks. 2) the remaining product diluted with an equal volume of molecular grade glycerol and stored at -20°C.
Usage Recommendations
While optimal Ig concentration for an application will vary, a good starting concentration for immunohistochemistry (IHC), immunofluorescence(IF) and staining is 2-5 µg/ml. For Western blots, the concentration is decreased by one order of magnitude (that is, 0.2-0.5 µg/ml).
All cell products contain the antimicrobial ProClin. Click here for additional information.

17 References

  • Initial Publication
  • IF References
  • WB References
  • IHC References
  • ELISA References
  • All References
  • Initial Publication
    IF References

    Structure-activity relationships in rodent diaphragm muscle fibers vs. neuromuscular junctions.
    Mantilla CB
    Respiratory physiology and neurobiology 180.1 (2012 Jan 15): 88-96.

    Specificity of different anti-myosin heavy chain antibodies in bovine muscle.
    Geay Y
    Meat science 55.1 (2000 May): 67-78.

    Evidence for differential post-translational modifications of slow myosin heavy chain during murine skeletal muscle development.
    Hughes SM
    Journal of muscle research and cell motility 21.2 (2000 Feb): 101-13.

    Evidence for myoblast-extrinsic regulation of slow myosin heavy chain expression during muscle fiber formation in embryonic development.
    Blau HM
    The Journal of cell biology 121.4 (1993 May): 795-810.

    IGF-1R Reduction Triggers Neuroprotective Signaling Pathways in Spinal Muscular Atrophy Mice.
    Charbonnier F
    The Journal of neuroscience : the official journal of the Society for Neuroscience 35.34 (2015 Aug 26): 12063-79.

    Regulation of myosin heavy chain expression during rat skeletal muscle development in vitro.
    Daniels MP
    Molecular biology of the cell 12.5 (2001 May): 1499-508.

    MyoD and myogenin protein expression in skeletal muscles of senile rats.
    Carlson BM
    Cell and tissue research 311.3 (2003 Mar): 401-16.

    Exercise-induced activation of NMDA receptor promotes motor unit development and survival in a type 2 spinal muscular atrophy model mouse.
    Charbonnier F
    The Journal of neuroscience : the official journal of the Society for Neuroscience 28.4 (2008 Jan 23): 953-62.

    Significant differences among skeletal muscles in the incorporation of bone marrow-derived cells.
    Blau HM
    Developmental biology 262.1 (2003 Oct 1): 64-74.

    WB References

    Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.
    Sokoloff AJ
    Muscle and nerve 49.4 (2014 Apr): 534-44.

    Specificity of different anti-myosin heavy chain antibodies in bovine muscle.
    Geay Y
    Meat science 55.1 (2000 May): 67-78.

    Postnatal development of myosin heavy chain isoforms in rat laryngeal muscles.
    Flint PW
    The Annals of otology, rhinology, and laryngology 108.5 (1999 May): 509-15.

    Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy.
    Blau HM
    Cell 52.4 (1988 Feb 26): 503-13.

    Evidence for myoblast-extrinsic regulation of slow myosin heavy chain expression during muscle fiber formation in embryonic development.
    Blau HM
    The Journal of cell biology 121.4 (1993 May): 795-810.

    Role of contraction duration in inducing fast-to-slow contractile and metabolic protein and functional changes in engineered muscle.
    Baar K
    Journal of cellular physiology 230.10 (2015 Oct): 2489-97.

    Respiratory muscle weakness in the Zucker diabetic fatty rat.
    Simpson JA
    American journal of physiology. Regulatory, integrative and comparative physiology 309.7 (2015 Oct): R780-7.

    Glucose concentration and streptomycin alter in vitro muscle function and metabolism.
    Baar K
    Journal of cellular physiology 230.6 (2015 Jun): 1226-34.

    Myosin heavy chain composition in human laryngeal muscles.
    Flint PW
    The Laryngoscope 109.9 (1999 Sep): 1521-4.

    IHC References
    ELISA References
    All References

    Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.
    Sokoloff AJ
    Muscle and nerve 49.4 (2014 Apr): 534-44.

    Evidence for differential post-translational modifications of slow myosin heavy chain during murine skeletal muscle development.
    Hughes SM
    Journal of muscle research and cell motility 21.2 (2000 Feb): 101-13.

    Muscle fiber pattern is independent of cell lineage in postnatal rodent development.
    Blau HM
    Cell 68.4 (1992 Feb 21): 659-71.

    Structure-activity relationships in rodent diaphragm muscle fibers vs. neuromuscular junctions.
    Mantilla CB
    Respiratory physiology and neurobiology 180.1 (2012 Jan 15): 88-96.

    Specificity of different anti-myosin heavy chain antibodies in bovine muscle.
    Geay Y
    Meat science 55.1 (2000 May): 67-78.

    Evidence for myoblast-extrinsic regulation of slow myosin heavy chain expression during muscle fiber formation in embryonic development.
    Blau HM
    The Journal of cell biology 121.4 (1993 May): 795-810.

    IGF-1R Reduction Triggers Neuroprotective Signaling Pathways in Spinal Muscular Atrophy Mice.
    Charbonnier F
    The Journal of neuroscience : the official journal of the Society for Neuroscience 35.34 (2015 Aug 26): 12063-79.

    Regulation of myosin heavy chain expression during rat skeletal muscle development in vitro.
    Daniels MP
    Molecular biology of the cell 12.5 (2001 May): 1499-508.

    MyoD and myogenin protein expression in skeletal muscles of senile rats.
    Carlson BM
    Cell and tissue research 311.3 (2003 Mar): 401-16.

    Exercise-induced activation of NMDA receptor promotes motor unit development and survival in a type 2 spinal muscular atrophy model mouse.
    Charbonnier F
    The Journal of neuroscience : the official journal of the Society for Neuroscience 28.4 (2008 Jan 23): 953-62.

    Significant differences among skeletal muscles in the incorporation of bone marrow-derived cells.
    Blau HM
    Developmental biology 262.1 (2003 Oct 1): 64-74.

    Postnatal development of myosin heavy chain isoforms in rat laryngeal muscles.
    Flint PW
    The Annals of otology, rhinology, and laryngology 108.5 (1999 May): 509-15.

    Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy.
    Blau HM
    Cell 52.4 (1988 Feb 26): 503-13.

    Role of contraction duration in inducing fast-to-slow contractile and metabolic protein and functional changes in engineered muscle.
    Baar K
    Journal of cellular physiology 230.10 (2015 Oct): 2489-97.

    Respiratory muscle weakness in the Zucker diabetic fatty rat.
    Simpson JA
    American journal of physiology. Regulatory, integrative and comparative physiology 309.7 (2015 Oct): R780-7.

    Glucose concentration and streptomycin alter in vitro muscle function and metabolism.
    Baar K
    Journal of cellular physiology 230.6 (2015 Jun): 1226-34.

    Myosin heavy chain composition in human laryngeal muscles.
    Flint PW
    The Laryngoscope 109.9 (1999 Sep): 1521-4.

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