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AB9660 Sigma-AldrichAnti-Tau phospho Serine 404 Antibody

Anti-Tau phospho Serine 404 Antibody is an antibody against Tau phospho Serine 404 for use in WB.

Anti-Tau phospho Serine 404 Antibody MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

SDS
CoA
References

Research Category: Neuroscience Research Sub-Category: Neurodegenerative Diseases Gene Symbol: MAPT, MTBT2, MAPTL, PHF-tau, tau, DDPAC, FTDP-17, MGC138549, MSTD, TAU, FLJ31424, MTBT1, PPND UniProt Number: P10636

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AB9660

100 µL 10 blots

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Key Specifications Table

Species Reactivity	Key Applications	Host	Format	Antibody Type
H	WB	Rb	Affinity Purified	Polyclonal Antibody

Description
Catalogue Number	AB9660
Brand Family	Chemicon®
Trade Name	Chemicon
Description	Anti-Tau phospho Serine 404 Antibody
Background Information	Tau is a neuronal microtubule-associated protein found predominantly on axons and functions to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer's disease (AD) brain. Hyperphosphorylated Tau is also found in neurofibrillary lesions in a range of other central nervous system disorders. Hyperphosphorylation impairs the microtubule binding function of Tau, resulting in the destabilization of microtubules in AD brains, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II (CK2), phosphorylate Tau. Serine 404 is phosphorylated by GSK-3beta and cdk5 in vitro and in vivo.

References

Product Information
Format	Affinity Purified
Presentation	Affinity purified immunoglobulin. Liquid in Dulbecco's PBS (without Mg²⁺and Ca²⁺), pH 7.3, 50% glycerol with 1.0 mg/mL BSA and 0.05% sodium azide.
Quality Level	MQ100

Applications
Application	Anti-Tau phospho Serine 404 Antibody is an antibody against Tau phospho Serine 404 for use in WB.
Key Applications	Western Blotting
Application Notes	Western blot: 1:1,000. Suggested blocking buffer is 5% BSA-TBST for one hour at room temperature. Suggested antibody dilution buffer is 3% BSA-TBST. Suggested antibody incubation time is 2 hours at room temperature. Optimal working dilutions must be determined by the end user.

Biological Information
Immunogen	Synthetic peptide of amino acids surrounding the phosphoSerine 404 site of human Tau.
Host	Rabbit
Specificity	Tau phosphoSerine 404. The antibody recognizes Tau pSerine 404 in samples of recombinant human Tau treated with GSK-3beta for 45 minutes. The reactivity of the antibody is blocked with the pSerine 404 peptide but not the non-phosphopeptide or a generic phosphoSerine-containing peptide.
Species Reactivity	Human
Antibody Type	Polyclonal Antibody
Entrez Gene Number	NM_005910.3 NM_016834.2 NM_016835.2 NM_016841.2
Entrez Gene Summary	This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
Gene Symbol	MAPT MTBT2 MAPTL PHF-tau tau DDPAC FTDP-17 MGC138549 MSTD TAU FLJ31424 MTBT1 PPND
Modifications	Phosphorylation
UniProt Number	P10636
UniProt Summary	FUNCTION: SwissProt: P10636 # 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 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. SIZE: 758 amino acids; 78878 Da SUBUNIT: Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. 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 is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain. DOMAIN: SwissProt: P10636 The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats. PTM: Phosphorylation at serine and threonine residues in S-P or T- P motifs by proline-directed protein kinases (PDPK: CDC2, CDK5, GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in PHF-tau), and at serine residues in K- X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) in Alzheimer diseased brains. Phosphorylation decreases with age. Phosphorylation within tau's repeat domain or in flanking regions seems to reduce tau'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. & 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. & Glycation of PHF-tau, but not normal brain tau. 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. DISEASE: SwissProt: P10636 # 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). & Defects in MAPT are a cause of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274, 172700]; also called frontotemporal dementia (FTD) or historically termed Pick complex. This form of frontotemporal dementia is characterized by 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. & Defects in MAPT are a cause of pallido-ponto-nigral degeneration (PPND) [MIM:168610]. The clinical features include ocular motility abnormalities, dystonia and urinary incontinence, besides progressive parkinsonism and dementia. & 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. & Defects in MAPT are a cause of progressive supranuclear palsy (PSP) [MIM:601104, 260540]; also known as Steele-Richardson- Olszewski syndrome. PSP is 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. & Defects in MAPT may be a cause of hereditary dysphasic disinhibition dementia (HDDD) [MIM:607485]. HDDD is a frontotemporal dementia characterized by progressive cognitive deficits with memory loss and personality changes, severe dysphasic disturbances leading to mutism, and hyperphagia. SIMILARITY: Contains 4 Tau/MAP repeats.

Physicochemical Information

Dimensions

Materials Information

Toxicological Information

Safety Information according to GHS

Safety Information

Product Usage Statements
Usage Statement	Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage and Shipping Information
Storage Conditions	Maintain at -20°C in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.

Packaging Information
Material Size	100 µL
Material Package	10 blots

Transport Information

Supplemental Information

Specifications

Global Trade Item Number
Catalog Number	GTIN
AB9660	04053252362071

Documentation

Anti-Tau phospho Serine 404 Antibody SDS

Title
Safety Data Sheet (SDS)

Anti-Tau phospho Serine 404 Antibody Certificates of Analysis

Title	Lot Number
RABBIT ANTI-Tau phosphoSerine 404 - 2095341	2095341
RABBIT ANTI-Tau phosphoSerine 404 - 3309567	3309567
RABBIT ANTI-Tau phosphoSerine 404 - 3407281	3407281
RABBIT ANTI-Tau phosphoSerine 404 - 3822752	3822752
RABBIT ANTI-Tau phosphoSerine 404 - 4187229	4187229
RABBIT ANTI-Tau phosphoSerine 404 POLYCLONAL ANTIBODY	3130464
RABBIT ANTI-Tau phosphoSerine 404 POLYCLONAL ANTIBODY	3130463
RABBIT ANTI-Tau phosphoSerine 404 POLYCLONAL ANTIBODY	2967213
RABBIT ANTI-Tau phosphoSerine 404 POLYCLONAL ANTIBODY - 2058950	2058950
RABBIT ANTI-Tau phosphoSerine 404 POLYCLONAL ANTIBODY - 2073622	2073622

References

Reference overview	Pub Med ID
Dephosphorylation of Tau by protein phosphatase 5: impairment in Alzheimer's disease. Liu, F., et al. J. Biol. Chem., 280(3):1790-1796 (2005) 2005	15546861
The retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cell line as a model for Alzheimer's disease-like tau phosphorylation. Jämsä, A., et al. Biochem. Biophys. Res. Comm., 319:993-1000 (2004) 2004	15184080
O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Liu, Fei, et al. Proc. Natl. Acad. Sci. U.S.A., 101: 10804-9 (2004) 2004 Show Abstract Microtubule-associated protein tau is abnormally hyperphosphorylated and aggregated into neurofibrillary tangles in brains of individuals with Alzheimer's disease (AD) and other tauopathies. Tau pathology is critical to pathogenesis and correlates to the severity of dementia. However, the mechanisms leading to abnormal hyperphosphorylation are unknown. Here, we demonstrate that human brain tau was modified by O-GlcNAcylation, a type of protein O-glycosylation by which the monosaccharide beta-N-acetylglucosamine (GlcNAc) attaches to serine/threonine residues via an O-linked glycosidic bond. O-GlcNAcylation regulated phosphorylation of tau in a site-specific manner both in vitro and in vivo. At most of the phosphorylation sites, O-GlcNAcylation negatively regulated tau phosphorylation. In an animal model of starved mice, low glucose uptake/metabolism that mimicked those observed in AD brain produced a decrease in O-GlcNAcylation and consequent hyperphosphorylation of tau at the majority of the phosphorylation sites. The O-GlcNAcylation level in AD brain extracts was decreased as compared to that in controls. These results reveal a mechanism of regulation of tau phosphorylation and suggest that abnormal hyperphosphorylation of tau could result from decreased tau O-GlcNAcylation, which probably is induced by deficient brain glucose uptake/metabolism in AD and other tauopathies.	15249677
Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Augustinack, J.C., et al. Acta Neuropathol., 103:26-35 (2002) 2002	11837744
Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. Liu, F., et al. FEBS Lett., 530(1-3):209-214 (2002) 2002	12387894
Site-specific phosphorylation of tau accompanied by activation of mitogen-activated protein kinase (MAPK) in brains of Niemann-Pick type C mice. Sawamura, N, et al. J. Biol. Chem., 276: 10314-9 (2001) 2001 Show Abstract Niemann-Pick type C (NPC) disease is characterized by an accumulation of cholesterol in most tissues and progressive neurodegeneration with the formation of neurofibrillary tangles. Neurofibrillary tangles are composed of paired helical filaments (PHF), a major component of which is the hyperphosphorylated tau. In this study we used NPC heterozygous and NPC homozygous mouse brains to investigate the molecular mechanism responsible for tauopathy in NPC. Immunoblot analysis using anti-tau antibodies (Tau-1, PHF-1, AT-180, and AT-100) revealed site-specific phosphorylation of tau at Ser-396 and Ser-404 in the brains of NPC homozygous mice. Mitogen-activated protein kinase, a potential serine kinase known to phosphorylate tau, was activated, whereas other serine kinases such as glycogen synthase kinase-3beta and cyclin-dependent kinase 5 were inactive. Morphological examination demonstrated that a number of neurons, the perikarya of which strongly immunostained with PHF-1, exhibited polymorphorous cytoplasmic inclusion bodies and multi-concentric lamellar-like bodies. Importantly, the accumulation of intracellular cholesterol in NPC mouse brains was determined to be a function of age. From these results we conclude that abnormal cholesterol metabolism due to the genetic mutation in NPC1 may be responsible for activation of the mitogen-activated protein kinase-signaling pathway and site-specific phosphorylation of tau in vivo, leading to tauopathy in NPC.	11152466
Expression of human apolipoprotein E4 in neurons causes hyperphosphorylation of protein tau in the brains of transgenic mice. Tesseur,I., et al. Am. J. Pathol., 156(3):951-964 (2000) 2000	10702411
Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease. Gong, C.X., et al. J. Biol. Chem., 275(8):5535-5544 (2000) 2000	10681533
Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. Wang, J.Z., et al. FEBS Lett., 436(1):28-34 (1998) 1998	9771888

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AB9660 Sigma-AldrichAnti-Tau phospho Serine 404 Antibody

Anti-Tau phospho Serine 404 Antibody is an antibody against Tau phospho Serine 404 for use in WB.

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Key Specifications Table

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Anti-Tau phospho Serine 404 Antibody SDS

Anti-Tau phospho Serine 404 Antibody Certificates of Analysis

References

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Anti-Tau phospho Serine 404 Antibody is an antibody against Tau phospho Serine 404 for use in WB.

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Key Specifications Table

Anti-Tau phospho Serine 404 Antibody SDS

Anti-Tau phospho Serine 404 Antibody Certificates of Analysis

References

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