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577814 PhosphoDetect™ Anti-Tau (pSer²⁶²) Rabbit pAb

577814
  
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Overview

Replacement Information

Key Spec Table

Host
Rb
Description
Overview

This product has been discontinued.





Recognizes the ~45-68 kDa Tau protein phosphorylated at Ser262.
Note: 1 T = 1 test.
Catalogue Number577814
Brand Family Calbiochem®
Application Data
Detection of human tau, phosphorylated at Ser262, by immunoblotting. Samples: Whole cell lysate from NIH3T3 cell with exogenously added human recombinant tau left untreated (lane 1) or treated with GSK-3β (lanes 2-5). Primary antibody: PhosphoDetect™ Anti-Tau (pSer262) Rabbit pAb (Cat. No. 577814) (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
ReferencesBennecib, M., et al. 2001. FEBS Lett. 490, 15.
del C. Alonso, A., et al. 2001. J. Biol. Chem. 276, 37967.
Sawamura, N., et al. 2001. J. Biol. Chem. 276, 10314.
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.
Jenkins, S.M., and Johnson, G.V. 2000. J. Neurochem. 74, 1463.
Maas, T., et al. 2000. J. Biol. Chem. 275, 15733.
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 PBS, 1 mg/ml BSA, 50% glycerol, pH 7.3.
Positive controlHuman recombinant tau treated with GSK-3β or OV-1 cells stably expressing human four-repeat tau and SV40 small Tantigen.
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. The immunogen sequence is 92% conserved in mouse and rat and 100% conserved in bovine, goat, baboon, and monkey tau. Variables associated with assay conditions will dictate the proper working dilution.
Biological Information
Immunogena synthetic phosphopeptide corresponding to amino acids surrounding the Ser²⁶² phosphorylation site of human Tau
ImmunogenHuman
HostRabbit
IsotypeIgG
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 Irritant
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
Catalogue Number GTIN
577814 0

Documentation

PhosphoDetect™ Anti-Tau (pSer²⁶²) Rabbit pAb Certificates of Analysis

TitleLot Number
577814

References

Reference overview
Bennecib, M., et al. 2001. FEBS Lett. 490, 15.
del C. Alonso, A., et al. 2001. J. Biol. Chem. 276, 37967.
Sawamura, N., et al. 2001. J. Biol. Chem. 276, 10314.
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.
Jenkins, S.M., and Johnson, G.V. 2000. J. Neurochem. 74, 1463.
Maas, T., et al. 2000. J. Biol. Chem. 275, 15733.
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 Ser262, by immunoblotting. Samples: Whole cell lysate from NIH3T3 cell with exogenously added human recombinant tau left untreated (lane 1) or treated with GSK-3β (lanes 2-5). Primary antibody: PhosphoDetect™ Anti-Tau (pSer262) Rabbit pAb (Cat. No. 577814) (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 Ser262.
BackgroundTau is the microtubule-associated protein found predominantly in neurons. It promotes the 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 both as a cytosolic protein and as polymerized paired helical filaments (PHF). The PHF form the building blocks for the 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 is the result of hyperphosphorylation of tau. Phosphorylation of tau at Thr231 by GSK-3 requires prior phosphorylation by protein kinase A at other sites. Phosphorylation at Thr231 and Ser262 is required for maximal inhibition of tau's binding to microtubules. CaM kinase II is the major kinase that phosphorylates Ser262 in the brain. Protein 14-3-3 ζ stimulates phosphorylation of Ser262 by protein kinase A.
HostRabbit
Immunogen speciesHuman
Immunogena synthetic phosphopeptide corresponding to amino acids surrounding the Ser²⁶² phosphorylation site of human Tau
IsotypeIgG
Specieshuman, mouse, rat
Positive controlHuman recombinant tau treated with GSK-3β or OV-1 cells stably expressing human four-repeat tau and SV40 small Tantigen.
FormLiquid
FormulationIn PBS, 1 mg/ml BSA, 50% glycerol, pH 7.3.
Preservative≤0.1% sodium azide
CommentsWhen used at a 1:1000 dilution, there is sufficient antibody for 10 immunoblots at 10 ml/blot. The immunogen sequence is 92% conserved in mouse and rat and 100% conserved in bovine, goat, baboon, and monkey tau. 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 Irritant
ReferencesBennecib, M., et al. 2001. FEBS Lett. 490, 15.
del C. Alonso, A., et al. 2001. J. Biol. Chem. 276, 37967.
Sawamura, N., et al. 2001. J. Biol. Chem. 276, 10314.
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.
Jenkins, S.M., and Johnson, G.V. 2000. J. Neurochem. 74, 1463.
Maas, T., et al. 2000. J. Biol. Chem. 275, 15733.
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.