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Category
Primary Antibodies
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Long description
This antibody recognizes tau when truncated at Asp421. Several caspases, including caspase-3, caspase-7, and caspase-8, cleave tau at this site, yielding the truncated form of the protein. This antibody does not react with full-length tau, or with tau truncated at Glu391 or Ala429. Tau is a microtubule-associated protein found predominantly in neuronal axons of vertebrate brain that promotes the assembly of tubulin monomers into microtubules and stabilizes microtubules. Hyperphosphorylation impairs the microtubule binding function of tau. Hyperphosphorylated tau is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in AlzheimerÕs disease (AD) brain. The truncation state of tau can influence many of its pathologic characteristics, including its ability to assume AD-related conformations and to assemble into filaments. Recent data suggest that A can trigger caspase activation and cell apoptosis. Caspase cleavage of tau at Asp 421 at the C-terminus is an important inducer of tau polymerization in Alzheimer's disease. This antibody provides a tool for studying neuronal cell apoptosis.
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Antibody come from
A chemically synthesized phosphopeptide derived from the region of human c-Jun that contains serine 73. The sequence is conserved among many species including mouse, rat and chicken.
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Other description
Provided as solution in phosphate buffered saline, pH 7.3, with 50% glycerol, 1.0 mg/ml BSA and 0.05% sodium azide. Protein A/G Chromatography
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Clone
TauC3
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Antigen antibody binding interaction
Mouse anti tau (421/422) Antibody
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Antibody is raised in
Mouse
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Antibody s reacts with
Human, Mouse, Rat
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Antibody s reacts with these species
This antibody doesn't cross react with other species
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Antibody s specificity
No Data Available
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Application
Western Blot, Immunoprecipitation, Immunohistochemistry
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Antibody s suited for
Optimal concentration should be evaluated by serial dilutions.Mouse reactive. Other species (100% homologous) have not been tested, but are expected to react due to sequence conservation. JunD (93%) was not detected in NIH3T3 cells, but may react in cells that express relatively high amounts of this protein. The antibody has been used in Western blotting. For Western blotting applications, we recommend using the antibody at a 1:1000 starting dilution. The optimal antibody concentration should be determined empirically for each specific application.
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Storage
-20ºC
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Relevant references
1. Vinciguerra, M., et al. (2004) Differential phosphorylation of c-Jun and JunD in response to the epidermal growth factor is determined by the structure of MAPK targeting sequences. J. Biol. Chem. 279(10):9634-_x000B_9641._x000B_2. David, J.P., et al. (2002) JNK1 modulates osteoclastogenesis through both c-Jun phosphorylation-dependent and -independent mechanisms. J. Cell. Sci. 115(Pt 22):4317-4325._x000B_3. Dunn, C., et al. (2002) Molecular mechanism and biological functions of c-Jun N-terminal kinase signaling via the c-Jun transcription factor. Cell. Signal. 14(7):585-593._x000B_4. Peterson, T.C., et al. (2002) Selective down-regulation of c-jun gene expression by pentoxifylline and c-jun antisense interrupts platelet-derived growth factor signaling: pentoxifylline inhibits phosphorylation of c-Jun on serine 73. Mol. Pharmacol. 61:1476-1488._x000B_5. Schwarz, C.S., et al. (2002) Bcl-2 up-regulates ha-ras mRNA expression and induces c-Jun phosphorylation at Ser73 via an ERK-dependent pathway in PC12 cells. Neuroreport 13(18):2439-2442._x000B_6. Bost, F., et al. (2001) The defective transforming phenotype of c-Jun Ala(63/73) is rescued by mutation of the C-terminal phosphorylation site. Oncogene 20(50):7425-7429._x000B_7. Leppa, S., et al. (2001) Complex functions of AP-1 transcription factors in differentiation and survival of PC12 cells. Mol. Cell. Biol. 21(13):4369-4378._x000B_8. De Ruiter, N.D., et al. (2000) Ras-dependent regulation of c-Jun phosphorylation is mediated by the Ral guanine nucleotide exchange factor-Ral pathway. Mol. Cell Biol. 20(22):8480-8488._x000B_9. Brecht, S., et al. (1999) Repetitive electroconvulsive seizures induce activity of c-Jun N-terminal kinase and compartment-specific desensitization of c-Jun phosphorylation in the rat brain. Brain Res. Mol. Brain Res. 68(1-2):101-108._x000B_10. Leppa, S. and D. Bohmann (1999) Diverse functions of JNK signaling and c-Jun in stress response and apoptosis. Oncogene 18(45):6158-6162._x000B_11. Herdegen, T., et al. (1998) Lasting N-terminal phosphorylation of c-Jun and activation of c-Jun N-terminal kinases after neuronal injury. J. Neurosci. 18(14):5124-5135.
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Protein number
see ncbi
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Warnings
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
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Description
This antibody needs to be stored at + 4°C in a fridge short term in a concentrated dilution. Freeze thaw will destroy a percentage in every cycle and should be avoided.
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Test
Mouse or mice from the Mus musculus species are used for production of mouse monoclonal antibodies or mabs and as research model for humans in your lab. Mouse are mature after 40 days for females and 55 days for males. The female mice are pregnant only 20 days and can give birth to 10 litters of 6-8 mice a year. Transgenic, knock-out, congenic and inbread strains are known for C57BL/6, A/J, BALB/c, SCID while the CD-1 is outbred as strain.
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Latin name
Mus musculus
