5A6

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$45.00
SKU: 5A6
View product citations for antibody 5A6 on CiteAb

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Available: 120

DSHB Data Sheet

Catalog Fields

Antigen: Tau
Hybridoma Cells Available: Yes
Antigen Species: Human
Depositor: Johnson, G.V.W.
Isotype: MIgG1
Antigen Sequence:
Host Species: mouse
Depositors Institution: University of Rochester Medical Center
Positive Tested Species Reactivity: Drosophila, Human
Depositors Notes:
Antigen Molecular Weight: 45-58 kDa
Human Protein Atlas:  
Predicted Species Reactivity:  
Gene: MAPT
Immunogen: human recombinant/longest brain isoform 441aa
Alternate Gene Names: MAPTL, MTBT1, TAU
Alternate Antibody Name:
Clonality: Monoclonal
Alternate Antigen Name:
Epitope Mapped: No
Myeloma Strain:
Epitope Location or Sequence: 19-46
Uniprot ID: P10636 
Immunogen Sequence:
Entrez Gene ID:  
Additional Characterization:  
Antibody Registry ID: AB_528487 
Additional Information:
Recommended Applications: Immunofluorescence, 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:
5A6 was deposited to the DSHB by Johnson, G.V.W. (DSHB Hybridoma Product 5A6)
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).
All cell products contain the antimicrobial ProClin. Click here for additional information.

13 References

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

    Serotonergic dystrophy induced by excess serotonin.
    Condron BG
    Molecular and cellular neurosciences 44.3 (2010 Jul): 297-306.

    Lrrk promotes tau neurotoxicity through dysregulation of actin and mitochondrial dynamics.
    Feany MB
    PLoS biology 16.12 (2018 Dec): e2006265.

    CCNA2 Ablation in Aged Mice Results in Abnormal rRNA Granule Accumulation in Hippocampus.
    Czeisler CM
    The American journal of pathology 189.2 (2019 Feb): 426-439.

    Tau Accumulation via Reduced Autophagy Mediates GGGGCC Repeat Expansion-Induced Neurodegeneration in Drosophila Model of ALS.
    Lu B
    Neuroscience bulletin 36.12 (2020 Dec): 1414-1428.

    WB References

    Embryonic stem cell-based modeling of tau pathology in human neurons.
    Koch P
    The American journal of pathology 182.5 (2013 May): 1769-79.

    The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments.
    Galasko D
    Journal of neurochemistry 68.1 (1997 Jan): 430-3.

    Insulin transiently increases tau phosphorylation: involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase.
    Johnson GV
    Journal of neurochemistry 72.2 (1999 Feb): 576-84.

    Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila.
    Lecourtois M
    Human molecular genetics 16.5 (2007 Mar 1): 555-66.

    Multiple-motor based transport and its regulation by Tau.
    Gross SP
    Proceedings of the National Academy of Sciences of the United States of America 104.1 (2007 Jan 2): 87-92.

    Tau Accumulation via Reduced Autophagy Mediates GGGGCC Repeat Expansion-Induced Neurodegeneration in Drosophila Model of ALS.
    Lu B
    Neuroscience bulletin 36.12 (2020 Dec): 1414-1428.

    Biotin rescues mitochondrial dysfunction and neurotoxicity in a tauopathy model.
    Feany MB
    Proceedings of the National Academy of Sciences of the United States of America 117.52 (2020 Dec 29): 33608-33618.

    Insulin-like growth factor 1 gene transfer for sporadic Alzheimer's disease: New evidence for trophic factor mediated hippocampal neuronal and synaptic recovery-based behavior improvement.
    Reggiani PC
    Hippocampus 31.10 (2021 Oct): 1137-1153.

    Biotin rescues mitochondrial dysfunction and neurotoxicity in a tauopathy model.
    Feany MB
    Proceedings of the National Academy of Sciences of the United States of America 117.52 (2020 Dec 29): 33608-33618.

    IP References

    The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments.
    Galasko D
    Journal of neurochemistry 68.1 (1997 Jan): 430-3.

    Aminopeptidases do not directly degrade tau protein.
    Hersh LB
    Molecular neurodegeneration 5. (2010 Nov 5): 48.

    Epitope Map References

    Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease.
    Binder LI
    The Journal of neuroscience : the official journal of the Society for Neuroscience 24.36 (2004 Sep 8): 7895-902.

    All References

    Serotonergic dystrophy induced by excess serotonin.
    Condron BG
    Molecular and cellular neurosciences 44.3 (2010 Jul): 297-306.

    Lrrk promotes tau neurotoxicity through dysregulation of actin and mitochondrial dynamics.
    Feany MB
    PLoS biology 16.12 (2018 Dec): e2006265.

    CCNA2 Ablation in Aged Mice Results in Abnormal rRNA Granule Accumulation in Hippocampus.
    Czeisler CM
    The American journal of pathology 189.2 (2019 Feb): 426-439.

    Tau Accumulation via Reduced Autophagy Mediates GGGGCC Repeat Expansion-Induced Neurodegeneration in Drosophila Model of ALS.
    Lu B
    Neuroscience bulletin 36.12 (2020 Dec): 1414-1428.

    Embryonic stem cell-based modeling of tau pathology in human neurons.
    Koch P
    The American journal of pathology 182.5 (2013 May): 1769-79.

    The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments.
    Galasko D
    Journal of neurochemistry 68.1 (1997 Jan): 430-3.

    Insulin transiently increases tau phosphorylation: involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase.
    Johnson GV
    Journal of neurochemistry 72.2 (1999 Feb): 576-84.

    Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila.
    Lecourtois M
    Human molecular genetics 16.5 (2007 Mar 1): 555-66.

    Multiple-motor based transport and its regulation by Tau.
    Gross SP
    Proceedings of the National Academy of Sciences of the United States of America 104.1 (2007 Jan 2): 87-92.

    Biotin rescues mitochondrial dysfunction and neurotoxicity in a tauopathy model.
    Feany MB
    Proceedings of the National Academy of Sciences of the United States of America 117.52 (2020 Dec 29): 33608-33618.

    Insulin-like growth factor 1 gene transfer for sporadic Alzheimer's disease: New evidence for trophic factor mediated hippocampal neuronal and synaptic recovery-based behavior improvement.
    Reggiani PC
    Hippocampus 31.10 (2021 Oct): 1137-1153.

    Aminopeptidases do not directly degrade tau protein.
    Hersh LB
    Molecular neurodegeneration 5. (2010 Nov 5): 48.

    Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease.
    Binder LI
    The Journal of neuroscience : the official journal of the Society for Neuroscience 24.36 (2004 Sep 8): 7895-902.

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