PRODUCT CODE: R1401-7

Tau Rabbit Polyclonal Antibody (R1401-7)

Applications

  • WB

  • ICC

  • IHC-P

REACTIVITY

  • Human

  • Mouse

  • Rat

Western blot analysis of Tau on human brain tissue lysate using anti-Tau antibody at 1/1,000 dilution.
  • Western blot analysis of Tau on human brain tissue lysate using anti-Tau antibody at 1/1,000 dilution.
  • ICC staining Tau in SHG-44 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
  • Immunohistochemical analysis of paraffin-embedded rat brain tissue using anti-Tau antibody. Counter stained with hematoxylin.
  • Immunohistochemical analysis of paraffin-embedded mouse brain tissue using anti-Tau antibody. Counter stained with hematoxylin.
Western blot analysis of Tau on human brain tissue lysate using anti-Tau antibody at 1/1,000 dilution.

Applications

  • WB

  • ICC

  • IHC-P

REACTIVITY

  • Human

  • Mouse

  • Rat

SPECIFICATIONS

Product Type

Rabbit polyclonal primary

Product Name

Tau Rabbit Polyclonal Antibody (R1401-7)

Immunogen

Synthetic peptide within n-terminal human tau.

Host

Rabbit

Positive Control

Human brain tissue, SHG-44, rat brain tissue, mouse brain tissue.

Conjugation

Unconjugated

Clonality

Polyclonal

PROPERTIES

Form

Liquid

Storage Condition

Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.

Storage Buffer

1*PBS (pH7.4), 0.2% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Concentration

1 ug/ul

PURIFICATION

Peptide affinity purified

MOLECULAR WEIGHT

50kDa

Isotype

IgG

APPLICATION DILUTION

  • WB

  • 1:500-1:2,000

  • ICC

  • 1:50-1:200

  • IHC-P

  • 1:50-1:200

TARGET

UNIPROT #

PROTEIN NAME

Tau

SYNONYMS

AI413597 antibody; AW045860 antibody; DDPAC antibody; FLJ31424 antibody; FTDP 17 antibody; G protein beta1/gamma2 subunit interacting factor 1 antibody; MAPT antibody; MAPTL antibody; MGC134287 antibody; MGC138549 antibody; MGC156663 antibody; Microtubule associated protein tau antibody; Microtubule associated protein tau isoform 4 antibody; Microtubule-associated protein tau antibody; MSTD antibody; Mtapt antibody; MTBT1 antibody; MTBT2 antibody; Neurofibrillary tangle protein antibody; Paired helical filament tau antibody; Paired helical filament-tau antibody; PHF tau antibody; PHF-tau antibody; PPND antibody; PPP1R103 antibody; Protein phosphatase 1, regulatory subunit 103 antibody; pTau antibody; RNPTAU antibody; TAU antibody; TAU_HUMAN antibody; Tauopathy and respiratory failure, included antibody

TISSUE SPECIFICITY

Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

DEVELOPMENTAL STAGE

Four-repeat (type II) TAU/MAPT is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) TAU/MAPT is found in both adult and fetal brain.

POST-TRANSLATIONAL MODIFICATION

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, MARK2, MARK3 or MARK4), 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.

SUBCELLULAR LOCATION

Cytoplasm

FUNCTION

Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are found mostly in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Other nervous system MAPs may perform similar functions, as suggested by tau knockout mice that did not show abnormalities in brain development - possibly because of compensation in tau deficiency by other MAPs. Six tau isoforms exist in human brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. Tau is a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. Phosphorylation has been reported on approximately 30 of these sites in normal tau proteins. Hyperphosphorylation of the tau protein (tau inclusions, pTau) can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies.