MW8

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$50.00
SKU: MW8

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DSHB Data Sheet

Catalog Fields

Clone ID/Product Name: MW8
Available to For-Profits: Yes
Alternate Antibody Name:
Gene Symbol: HTT
Ab Isotype: MIgG2a
Gene Name:
Antibody Registry ID: AB_528297 
Uniprot ID: P42858 
RRID:  
Entrez Gene ID: 3064 
Clonality: Monoclonal
Immunogen: Hd exon-1 67Q aggregate
Clone:
Immunogen Sequence: HDx-67Q
Myeloma Strain: HL-1
Epitope Mapped: Yes
Antigen Name: Huntingtin
Epitope Location or Sequence: AEEPLHRPK/ a.a. 83-90
Alternate Antigen Name:
Deposit Date: 1/23/2003
Antigen Molecular Weight: 347.6 kDa
Depositor: Patterson, P.H.
Antigen Sequence:
Depositor Institution: California Institute of Technology
Antigen Species: Human
Depositor Notes: The MW8 exclusively stains aggregates as inclusions in both nuclei and in the neuropil. This antigen is also known as huntington disease protein.
Host Species: mouse
Hybridoma Cells Available (Non-Profit): Yes
Confirmed Species Reactivity: Human, Mouse
Additional Information: RRID:AB_528297; Time-resolved Förster resonance energy transfer (TR-FRET) assay has been developed using MW8 to assay huntingtin aggregates. PMID: 22365609 22984513
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:
MW8 was deposited to the DSHB by Patterson, P.H. (DSHB Hybridoma Product MW8)
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).

18 References

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

    Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity.
    Patterson PH
    Proceedings of the National Academy of Sciences of the United States of America 99.2 (2002 Jan 22): 1002-7.

    Mutant huntingtin gene-dose impacts on aggregate deposition, DARPP32 expression and neuroinflammation in HdhQ150 mice.
    Schmid P
    PloS one 8.9 (2013): e75108.

    Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging.
    Lotz GP
    PloS one 7.9 (2012): e44457.

    Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice.
    Zeitlin SO
    PLoS genetics 6.2 (2010 Feb 5): e1000838.

    Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.
    Muchowski PJ
    The Journal of biological chemistry 284.32 (2009 Aug 7): 21647-58.

    Differential morphology and composition of inclusions in the R6/2 mouse and PC12 cell models of Huntington's disease.
    Morton AJ
    Histochemistry and cell biology 127.5 (2007 May): 473-84.

    Identifying polyglutamine protein species in situ that best predict neurodegeneration.
    Finkbeiner S
    Nature chemical biology 7.12 (2011 Oct 30): 925-34.

    Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease.
    Bates GP
    The Journal of biological chemistry 285.12 (2010 Mar 19): 8808-23.

    Huntington's Disease Pathogenesis Is Modified In Vivo by Alfy/Wdfy3 and Selective Macroautophagy.
    Yamamoto A
    Neuron 105.5 (2020 Mar 4): 813-821.e6.

    WB References
    IHC References
    IP References
    ELISA References
    Epitope Map References
    All References

    New anti-huntingtin monoclonal antibodies: implications for huntingtin conformation and its binding proteins.
    Patterson PH
    Brain research bulletin 56.3-4 (2001 Oct-Nov 1): 319-29.

    Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice.
    Zeitlin SO
    PLoS genetics 6.2 (2010 Feb 5): e1000838.

    A series of N-terminal epitope tagged Hdh knock-in alleles expressing normal and mutant huntingtin: their application to understanding the effect of increasing the length of normal Huntingtin's polyglutamine stretch on CAG140 mouse model pathogenesis.
    Zeitlin SO
    Molecular brain 5. (2012 Aug 14): 28.

    Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models.
    Thompson LM
    The Journal of neuroscience : the official journal of the Society for Neuroscience 32.32 (2012 Aug 8): 11109-19.

    Human mutant huntingtin disrupts vocal learning in transgenic songbirds.
    Lee R
    Nature neuroscience 18.11 (2015 Nov): 1617-22.

    Comparison of mHTT Antibodies in Huntington's Disease Mouse Models Reveal Specific Binding Profiles and Steady-State Ubiquitin Levels with Disease Development.
    Brooks SP
    PloS one 11.5 (2016): e0155834.

    Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity.
    Patterson PH
    Proceedings of the National Academy of Sciences of the United States of America 99.2 (2002 Jan 22): 1002-7.

    Mutant huntingtin gene-dose impacts on aggregate deposition, DARPP32 expression and neuroinflammation in HdhQ150 mice.
    Schmid P
    PloS one 8.9 (2013): e75108.

    Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging.
    Lotz GP
    PloS one 7.9 (2012): e44457.

    Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.
    Muchowski PJ
    The Journal of biological chemistry 284.32 (2009 Aug 7): 21647-58.

    Differential morphology and composition of inclusions in the R6/2 mouse and PC12 cell models of Huntington's disease.
    Morton AJ
    Histochemistry and cell biology 127.5 (2007 May): 473-84.

    Identifying polyglutamine protein species in situ that best predict neurodegeneration.
    Finkbeiner S
    Nature chemical biology 7.12 (2011 Oct 30): 925-34.

    Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease.
    Bates GP
    The Journal of biological chemistry 285.12 (2010 Mar 19): 8808-23.

    Huntington's Disease Pathogenesis Is Modified In Vivo by Alfy/Wdfy3 and Selective Macroautophagy.
    Yamamoto A
    Neuron 105.5 (2020 Mar 4): 813-821.e6.

    TR-FRET-based duplex immunoassay reveals an inverse correlation of soluble and aggregated mutant huntingtin in huntington's disease.
    Weiss A
    Chemistry & biology 19.2 (2012 Feb 24): 264-75.

    Mitochondrial membranes modify mutant huntingtin aggregation.
    Legleiter J
    Biochimica et biophysica acta. Biomembranes 1863.10 (2021 Oct 1): 183663.

    Native mutant huntingtin in human brain: evidence for prevalence of full-length monomer.
    DiFiglia M
    The Journal of biological chemistry 287.16 (2012 Apr 13): 13487-99.

    Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core.
    van der Wel PCA
    Nature communications 8. (2017 May 24): 15462.

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