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Rabbit Polyclonal Anti-Tau (Acetyl Lys174) antibody (STJ98828)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-2000; ELISA 1:5000-20000
Recommended protocols: check protocols
Click or hover above images to see image description for Anti-Tau (Acetyl Lys174) antibody.
Check alternative names for the antibodyExpand
|FTDP17 antibody|Microtubule associated protein tau antibody|Paired helical filament tau antibody|PHF tau antibody|PPND antibody|TAU antibody|Anti-Tau 13 antibody [B11E8] (ab19030)
SCBT cat No: sc-66177|sc-271076|sc-5863|sc-166114|sc-166314|sc-28240|sc-166332|sc-5860|sc-80900|sc-53596|sc-18167|sc-365091|sc-514453|sc-15323|sc-14116|sc-14115|sc-5218|sc-5220|sc-14121|sc-22050|sc-28951|sc-14128|sc-28952|sc-168757|sc-161946|sc-161948|sc-20980|sc-514774|sc-21547|
Anti-Tau (Acetyl Lys174) antibody
|Catalogue No.|| |
Human, Mouse, Rat
Anti-Tau (Acetyl Lys174) antibody detects endogenous Tau when Acetyl occurs at Lys174.
Synthetic Acetyl peptide from human protein at AA range: 174.
|Recommended dilution|| |
WB 1:500-2000; ELISA 1:5000-20000
|Molecular weight|| |
Anti-Tau (Acetyl Lys174) antibody was tube-contained in PBS, pH 7.4, containing 0.02% sodium azide as Preservative and 50% Glycerol.
Anti-Tau (Acetyl Lys174) antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
FTDP17 antibody, Microtubule associated protein tau antibody, Paired helical filament tau antibody, PHF tau antibody, PPND antibody, TAU antibody
|Database links|| |
|Protein 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 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.
|Involvement in disease|| |
Note=In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). O-GlcNAcylation is greatly reduced in Alzheimer disease brain cerebral cortex leading to an increase in TAU/MAPT phosphorylations. .; Frontotemporal dementia (FTD) [MIM:600274]: A form of dementia characterized by pathologic finding of frontotemporal lobar degeneration, presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. . Note=The disease is caused by mutations affecting the gene represented in this entry.; Pick disease of the brain (PIDB) [MIM:172700]: A rare form of dementia pathologically defined by severe atrophy, neuronal loss and gliosis. It is characterized by the occurrence of tau-positive inclusions, swollen neurons (Pick cells) and argentophilic neuronal inclusions known as Pick bodies that disproportionally affect the frontal and temporal cortical regions. Clinical features include aphasia, apraxia, confusion, anomia, memory loss and personality deterioration. . Note=The disease is caused by mutations affecting the gene represented in this entry.; Note=Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease.; Progressive supranuclear palsy 1 (PSNP1) [MIM:601104]: Characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613. . Note=The disease is caused by mutations affecting the gene represented in this entry.; Parkinson-dementia syndrome (PARDE) [MIM:260540]: A syndrome characterized by parkinsonism, tremor, rigidity, dementia, ophthalmoparesis and pyramidal signs. Neurofibrillary degeneration occurs in the hippocampus, basal ganglia and brainstem nuclei. Note=The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
Contains 4 Tau/MAP repeats. The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.
|Protein 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 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.
|Protein cellular localization|| |
Cytoplasm, cytosol . Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm, cytoskeleton . Cell projection, axon . Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.
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St John’s Laboratory Ltd.
|Product type|| |
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