577815 PhosphoDetect™ Anti-Tau (pSer³⁹⁶) Rabbit pAb

577815
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Overview

Replacement Information

Key Specifications Table

Species ReactivityHostAntibody Type
H Rb Polyclonal Antibody

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577815-10T
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      Description
      OverviewRecognizes the ~45-68 kDa Tau protein phosphorylated at Ser396.
      Catalogue Number577815
      Brand Family Calbiochem®
      Application Data
      Detection of human tau, phosphorylated at Ser396, by immunoblotting. Samples: Whole cell lysate from control cells with exogenously added human recombinant tau left untreated (lane 1) or treated with GSK-3β (lanes 2-5). Primary antibody: PhosphoDetect™ Anti-Tau (pSer396) Rabbit pAb (Cat. No. 577815) (1:1000) pre-incubated without peptide (lanes 1, 2), with non-phosphopeptide corresponding to the immunogen (lane 3), a generic phosphoserine containing peptide (lane 4), or phosphopeptide immunogen (lane 5). Detection: chemiluminescence.
      References
      Referencesdel C. Alonso, A., et al. 2001. J. Biol. Chem. 276, 37967.
      Bennecib, M., et al. 2001. FEBS Lett. 490, 15.
      Sawamura, N., et al. 2001. J. Biol. Chem. 276, 10314.
      Tomidokoro, Y., et al. 2001. Neurosci. Lett. 299, 169.
      Bennecib, M., et al. 2000. FEBS Lett. 485, 87.
      Hashiguchi, M., et al. 2000. J. Biol. Chem. 275, 25247.
      Jenkins, S.M., et al. 2000. Biochem. J. 345, 263.
      Maas, T., et al., 2000. J. Biol. Chem. 275, 15733.
      Takahashi, M., et al. 2000. Brain. Res. 857, 193.
      Tesseur, I., et al. 2000. Am. J. Pathol. 156, 951.
      Schneider, A., et al. 1999. Biochemistry 38, 3549.
      Sengupta, A., et al. 1998. Arch. Biochem. Biophys. 357, 299.
      Wang, J.G., et al. 1998. FEBS Lett. 436, 28.
      Kopke, E., et al. 1993. J. Biol. Chem. 268, 24374.
      Arigada, P.A., et al. 1992. Neurology 42, 631.
      Drubin, D.G. and Kirschner, M.W. 1986. J. Cell. Biol. 103, 2739.
      Product Information
      FormLiquid
      FormulationIn Dulbecco's PBS (without Mg2+ and Ca2+), 1 mg/ml BSA, 50% glycerol, pH 7.2-7.4.
      Positive controlRecombinant human tau treated with GSK-3β
      Preservative≤0.1% sodium azide
      Quality LevelMQ100
      Applications
      Key Applications Immunoblotting (Western Blotting)
      Application NotesImmunoblotting (1:1000)
      Application CommentsWhen used at a 1:1000 dilution, there is sufficient antibody for 10 immunoblots at 10 ml/blot. Variables associated with assay conditions will dictate the proper working dilution.
      Biological Information
      Immunogena synthetic phosphopeptide corresponding to amino acids surrounding the Ser³⁹⁶ phosphorylation site of human Tau
      ImmunogenHuman
      HostRabbit
      IsotypeIgG
      Species Reactivity
      • Human
      Antibody TypePolyclonal Antibody
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Standard Handling
      Storage -20°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      PhosphoDetect™ Anti-Tau (pSer³⁹⁶) Rabbit pAb Certificates of Analysis

      TitleLot Number
      577815

      References

      Reference overview
      del C. Alonso, A., et al. 2001. J. Biol. Chem. 276, 37967.
      Bennecib, M., et al. 2001. FEBS Lett. 490, 15.
      Sawamura, N., et al. 2001. J. Biol. Chem. 276, 10314.
      Tomidokoro, Y., et al. 2001. Neurosci. Lett. 299, 169.
      Bennecib, M., et al. 2000. FEBS Lett. 485, 87.
      Hashiguchi, M., et al. 2000. J. Biol. Chem. 275, 25247.
      Jenkins, S.M., et al. 2000. Biochem. J. 345, 263.
      Maas, T., et al., 2000. J. Biol. Chem. 275, 15733.
      Takahashi, M., et al. 2000. Brain. Res. 857, 193.
      Tesseur, I., et al. 2000. Am. J. Pathol. 156, 951.
      Schneider, A., et al. 1999. Biochemistry 38, 3549.
      Sengupta, A., et al. 1998. Arch. Biochem. Biophys. 357, 299.
      Wang, J.G., et al. 1998. FEBS Lett. 436, 28.
      Kopke, E., et al. 1993. J. Biol. Chem. 268, 24374.
      Arigada, P.A., et al. 1992. Neurology 42, 631.
      Drubin, D.G. and Kirschner, M.W. 1986. J. Cell. Biol. 103, 2739.
      Data Sheet

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision16-August-2007 RFH
      ApplicationImmunoblotting (1:1000)
      Application Data
      Detection of human tau, phosphorylated at Ser396, by immunoblotting. Samples: Whole cell lysate from control cells with exogenously added human recombinant tau left untreated (lane 1) or treated with GSK-3β (lanes 2-5). Primary antibody: PhosphoDetect™ Anti-Tau (pSer396) Rabbit pAb (Cat. No. 577815) (1:1000) pre-incubated without peptide (lanes 1, 2), with non-phosphopeptide corresponding to the immunogen (lane 3), a generic phosphoserine containing peptide (lane 4), or phosphopeptide immunogen (lane 5). Detection: chemiluminescence.
      DescriptionRabbit polyclonal antibody adsorbed against non-phosphopeptide corresponding to the immunogen phosphorylation site, followed by immunoaffinity chromatography. Recognizes the ~45-68 kDa Tau protein phosphorylated at Ser396.
      BackgroundTau is the microtubule-associated protein predominantly found in neurons. It promotes assembly of tubulin into microtubules. Tau is also a phosphoprotein and its biological activity is regulated by the degree of phosphorylation. In the brain of Alzheimer's patients, tau is hyperphosphorylated and exists as both a cytosolic protein and as polymerized paired helical filaments (PHF). The PHF form the building blocks for neurofibrillary tangles that are the hallmark of AD brains. Hyperphosphorylated tau in AD inhibits the assembly of microtubules and causes disassembly of preassembled microtubules. Ultimately, hyperphosphorylated tau leads to the degeneration of the neurons and forms the pathogenic mechanism for Alzheimer's disease. In addition to AD brains, neurofibrillary tangles have also been observed in brains of patients with Niemann-Pick type C (NPC) disease. NPC is associated with the accumulation of cholesterol in several tissues and with progressive neurodegeneration. It has recently been shown that brains of NPC patients also accumulate neurofibrillary tangles without amyloid deposits. As in AD brains, the PHF of NPC brains are the result of hyperphosphorylation of tau. In tau, serine 396 is one of the four most prominent phosphorylation sites used by GSK-3.
      HostRabbit
      Immunogen speciesHuman
      Immunogena synthetic phosphopeptide corresponding to amino acids surrounding the Ser³⁹⁶ phosphorylation site of human Tau
      IsotypeIgG
      Specieshuman
      Positive controlRecombinant human tau treated with GSK-3β
      FormLiquid
      FormulationIn Dulbecco's PBS (without Mg2+ and Ca2+), 1 mg/ml BSA, 50% glycerol, pH 7.2-7.4.
      Preservative≤0.1% sodium azide
      CommentsWhen used at a 1:1000 dilution, there is sufficient antibody for 10 immunoblots at 10 ml/blot. Variables associated with assay conditions will dictate the proper working dilution.
      Storage -20°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Toxicity Standard Handling
      Referencesdel C. Alonso, A., et al. 2001. J. Biol. Chem. 276, 37967.
      Bennecib, M., et al. 2001. FEBS Lett. 490, 15.
      Sawamura, N., et al. 2001. J. Biol. Chem. 276, 10314.
      Tomidokoro, Y., et al. 2001. Neurosci. Lett. 299, 169.
      Bennecib, M., et al. 2000. FEBS Lett. 485, 87.
      Hashiguchi, M., et al. 2000. J. Biol. Chem. 275, 25247.
      Jenkins, S.M., et al. 2000. Biochem. J. 345, 263.
      Maas, T., et al., 2000. J. Biol. Chem. 275, 15733.
      Takahashi, M., et al. 2000. Brain. Res. 857, 193.
      Tesseur, I., et al. 2000. Am. J. Pathol. 156, 951.
      Schneider, A., et al. 1999. Biochemistry 38, 3549.
      Sengupta, A., et al. 1998. Arch. Biochem. Biophys. 357, 299.
      Wang, J.G., et al. 1998. FEBS Lett. 436, 28.
      Kopke, E., et al. 1993. J. Biol. Chem. 268, 24374.
      Arigada, P.A., et al. 1992. Neurology 42, 631.
      Drubin, D.G. and Kirschner, M.W. 1986. J. Cell. Biol. 103, 2739.

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