anti-Tau antibody

anti-Tau antibody for ICC/IF,Western blot and Human,Mouse,Rat

Neuroscience antibody; Signaling Transduction antibody; Neuron Development Study antibody


Product Description Chicken Polyclonal antibody recognizes Tau
Tested Reactivity Hu, Ms, Rat
Tested Application ICC/IF, WB
Host Chicken
Clonality Polyclonal
Isotype IgY
Target Name Tau
Antigen Species Human
Immunogen Recombinant full length 441 amino acid human tau isoform 2 (NP_005901.2) expressed in and purified from E.Coli.
Conjugation Un-conjugated
Alternate Names TAU; Neurofibrillary tangle protein; Paired helical filament-tau; PPND; DDPAC; FTDP-17; MTBT2; Microtubule-associated protein tau; PHF-tau; MSTD; PPP1R103; MTBT1; MAPTL

Application Instructions

Application Suggestion
Tested Application Dilution
ICC/IF1:1000 - 1:2000
WB1:5000 - 1:10000
Application Note Specific for the ~48, 65 & 75k tau isoforms.
* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.


Form Liquid
Purification Total IgY fraction
Buffer Total IgY fraction in PBS and 10 mM Sodium azide
Preservative 10 mM Sodium azide
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.


Database Links

GeneID: 17762 Mouse MAPT

GeneID: 29477 Rat MAPT

GeneID: 4137 Human MAPT

Gene Symbol MAPT
Gene Full Name microtubule-associated protein tau
Background Tau is a key microtubule-associated protein that plays an important role in the formation of microtubules in axons (Binder et al. 1985). Six tau isoforms have been identified as products of a single gene produced by alternative mRNA splicing (Goedert 1990). Tau mutations have been implicated in many neurodegenerative disorders such as Alzheimer’s disease (AD), Pick’s disease and progressive supranuclear palsy
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Neuronal Development Marker
Research Area Neuroscience antibody; Signaling Transduction antibody; Neuron Development Study antibody
Calculated MW 79 kDa
PTM Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1: CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Phosphorylation decreases with age. Phosphorylation within tau/MAP's repeat domain or in flanking regions seems to reduce tau/MAP's interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis. Phosphorylation at Ser-548 by GSK3B reduces ability to bind and stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons. There is a reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces glycosylation by a factor of 2 and 4 respectively. Phosphorylation on Ser-721 is reduced by about 41.5% by GlcNAcylation on Ser-717. Dephosphorylated at several serine and threonine residues by the serine/threonine phosphatase PPP5C.
Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur.
O-glycosylated. O-GlcNAcylation content is around 8.2%. There is reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces O-GlcNAcylation by a factor of 2 and 4 respectively. O-GlcNAcylation on Ser-717 decreases the phosphorylation on Ser-721 by about 41.5%.
Glycation of PHF-tau, but not normal brain TAU/MAPT. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD.

Images (2) Click the Picture to Zoom In

  • ARG52441 anti-Tau antibody ICC/IF image

    Immunofluorescence: cultured rat hippocampal neurons stained with Tau antibody (ARG52441) showing staining of tau in red along the neuronal processes.

  • ARG52441 anti-Tau antibody WB image

    Western Blot: rat cortex lysate stained with Tau antibody (ARG52441) showing specific immunolabeling of the ~48, 65 & 75k tau isoforms.