• Western blot analysis of lysates from rat brain, using Tau (Phospho-Thr534/217) Antibody. The lane on the right is blocked with the phospho peptide.

Anti-Phospho-MAPT-Thr534 antibody (181-230 aa) (STJ90577)

SKU:
STJ90577

Current Stock:
Host: Rabbit
Applications: WB/IHC/IF/ELISA
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-Phospho-Microtubule-associated protein tau-Thr534 (181-230 aa) is suitable for use in Western Blot, Immunohistochemistry, Immunofluorescence and ELISA research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide.
Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration: 1 mg/mL
Dilution Range: WB 1:500-1:2000
IHC 1:100-1:300
ELISA 1:5000
IF 1:50-200
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: MAPT
Gene ID: 4137
Uniprot ID: TAU_HUMAN
Immunogen Region: 181-230 aa
Specificity: Phospho-Tau (T534) Polyclonal Antibody detects endogenous levels of Tau protein only when phosphorylated at T534.
Immunogen: The antiserum was produced against synthesized peptide derived from the human Tau around the phosphorylation site of Thr534/217 at the amino acid range 181-230
Post Translational Modifications 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. 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.
Function Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
Protein Name Microtubule-Associated Protein Tau
Neurofibrillary Tangle Protein
Paired Helical Filament-Tau
Phf-Tau
Database Links Reactome: R-HSA-264870
Reactome: R-HSA-9619483 P10636-8
Cellular Localisation Cytoplasm
Cytosol
Cell Membrane
Peripheral Membrane Protein
Cytoplasmic Side
Cytoskeleton
Cell Projection
Axon
Dendrite
Secreted
Mostly Found In The Axons Of Neurons
In The Cytosol And In Association With Plasma Membrane Components
Can Be Secreted
The Secretion Is Dependent On Protein Unfolding And Facilitated By The Cargo Receptor Tmed10
It Results In Protein Translocation From The Cytoplasm Into The Ergic (Endoplasmic Reticulum-Golgi Intermediate Compartment) Followed By Vesicle Entry And Secretion
Alternative Antibody Names Anti-Microtubule-Associated Protein Tau antibody
Anti-Neurofibrillary Tangle Protein antibody
Anti-Paired Helical Filament-Tau antibody
Anti-Phf-Tau antibody
Anti-MAPT antibody
Anti-MAPTL antibody
Anti-MTBT1 antibody
Anti-TAU antibody

Information sourced from Uniprot.org

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