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577815 PhosphoDetect™ Anti-Tau (pSer³⁹⁶) Rabbit pAb

This PhosphoDetect™ Anti-Tau (pSer³⁹⁶) Rabbit pAb is validated for use in Immunoblotting for the detection of Tau (pSer³⁹⁶).

PhosphoDetect™ Anti-Tau (pSer³⁹⁶) Rabbit pAb : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
577815
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Aperçu

Replacement Information

Tableau de caractéristiques principal

Species ReactivityHostAntibody Type
HRbPolyclonal Antibody

Products

RéférenceConditionnement Qté
577815-10T Ampoule plast. 10 t
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
Global Trade Item Number
Référence GTIN
577815-10T 04055977265927

Documentation

PhosphoDetect™ Anti-Tau (pSer³⁹⁶) Rabbit pAb Certificats d'analyse

TitreNuméro de lot
577815

Références bibliographiques

Aperçu de la référence bibliographique
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.
Fiche technique

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 Avoid freeze/thaw
-20°C
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.