N3.36

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SKU: N3.36

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DSHB Data Sheet

Catalog Fields

Clone ID/Product Name: N3.36
Available to For-Profits: Yes
Alternate Antibody Name:
Gene Symbol: MYH8
Ab Isotype: MIgM
Gene Name:
Antibody Registry ID: AB_528380 
Uniprot ID: P13535 
RRID:  
Entrez Gene ID: 4626 
Clonality: Monoclonal
Immunogen: partially purified myosin (pyrophosphate extracted) from human neonatal (5 days old) skeletal muscle
Clone:
Immunogen Sequence:
Myeloma Strain: SP2/2
Epitope Mapped: Yes
Antigen Name: Myosin heavy chain Type IIA fast and human neonatal
Epitope Location or Sequence: Heavy meromyosin subfragment
Alternate Antigen Name:
Deposit Date: 8/25/1993
Antigen Molecular Weight: 220kDa
Depositor: Blau, H.M.
Antigen Sequence:
Depositor Institution: Stanford University, Baxter Lab for Stem Cell Biology
Antigen Species: Human
Depositor Notes: Fusion: 1983. Recognizes neonatal and adult fast fibers.
Host Species: mouse
Hybridoma Cells Available (Non-Profit): Yes
Confirmed Species Reactivity: Bovine, Human, Rat, Rodent
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.
Predicted Species Reactivity:  
Human Protein Atlas:  
Additional Characterization:  
Recommended Applications: ELISA, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot
All cell products contain the antimicrobial ProClin. Click here for additional information.
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. For immediate use, short term storage at 4°C up to two weeks is recommended. For long term storage, divide the solution into volumes of no less than 20 ul for freezing at -20°C or -80°C. The small volume aliquot should provide sufficient reagent for short term use. Freeze-thaw cycles should be avoided. For concentrate or bioreactor products, an equal volume of glycerol, a cryoprotectant, may be added prior to freezing.
Usage Recommendations
The optimal Ig concentration for an application varies by species and antibody affinity. For each product, the antibody titer must be optimized for every application by the end user laboratory. A good starting concentration for immunohistochemistry (IHC), immunofluorescence (IF), and immunocytochemistry (ICC) when using mouse Ig is 2-5 ug/ml. For western blots, the recommended concentration range of mouse Ig 0.2-0.5 ug/ml. In general, rabbit antibodies demonstrate greater affinity and are used at a magnitude lower Ig concentration for initial testing. The recommended concentrations for rabbit Ig are 0.2-0.5 ug/ml (IF, IHC and ICC) and 20-50 ng/ml (WB).

19 References

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

    Structure-activity relationships in rodent diaphragm muscle fibers vs. neuromuscular junctions.
    Mantilla CB
    Respiratory physiology & 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.

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

    WB References

    Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.
    Sokoloff AJ
    Muscle & 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.

    Fast myosin heavy chains expressed in secondary mammalian muscle fibers at the time of their inception.
    Blau HM
    Journal of cell science 107 ( Pt 9). (1994 Sep): 2361-71.

    IHC References
    ELISA References
    Epitope Map References
    All References

    Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.
    Sokoloff AJ
    Muscle & 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.

    Fast myosin heavy chains expressed in secondary mammalian muscle fibers at the time of their inception.
    Blau HM
    Journal of cell science 107 ( Pt 9). (1994 Sep): 2361-71.

    Structure-activity relationships in rodent diaphragm muscle fibers vs. neuromuscular junctions.
    Mantilla CB
    Respiratory physiology & 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.

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

    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.

    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.

    Developmental progression of myosin gene expression in cultured muscle cells.
    Blau HM
    Cell 46.7 (1986 Sep 26): 1075-81.

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