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AB9674 Sigma-AldrichAnti-Tau phospho Serine 199/202 Antibody

Detect Tau phospho Serine 199/202 using this Anti-Tau phospho Serine 199/202 Antibody validated for use in WB.

Anti-Tau phospho Serine 199/202 Antibody MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

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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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Key Spec Table

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

Description
Catalogue Number	AB9674
Brand Family	Chemicon®
Trade Name	Chemicon
Description	Anti-Tau phospho Serine 199/202 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. Serines 199 and 202 are phosphorylated by GSK-3beta and have been linked to hereditary frontotemporal dementia. Serine 202 phosphorylation by cdk5, stimulated by the presence of microtubules, has been linked to hereditary neurodegenerative disease.

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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	Detect Tau phospho Serine 199/202 using this Anti-Tau phospho Serine 199/202 Antibody validated for use in WB.
Key Applications	Western Blotting
Application Notes	Western blot: 1:1,000. Suggested blocking buffer is 5% BSA-TBST overnight at 2-8°C. 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 199 and 202 sites of human Tau.
Host	Rabbit
Specificity	Tau phosphoSerine 199/202. The antibody recognizes Tau pSerine 199/202 in samples of recombinant human Tau treated with GSK-3beta for 45 minutes. The reactivity of the antibody is blocked with the pSerine 199/202 peptide but not the non-phosphopeptide, tau phosphopeptide corresponding to pSerine 199, tau phosphopeptide corresponding to pSerine 202 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.

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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

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Supplemental Information

Specifications

Global Trade Item Number
Catalogue Number	GTIN
AB9674	04053252512070

Documentation

Anti-Tau phospho Serine 199/202 Antibody MSDS

Title
Safety Data Sheet (SDS)

Anti-Tau phospho Serine 199/202 Antibody Certificates of Analysis

Title	Lot Number
RABBIT ANTI-Tau phosphoSerine 199/202 - 2492184	2492184
RABBIT ANTI-Tau phosphoSerine 199/202 - 3202917	3202917
RABBIT ANTI-Tau phosphoSerine 199/202 - 3238461	3238461
RABBIT ANTI-Tau phosphoSerine 199/202 - 3252936	3252936
RABBIT ANTI-Tau phosphoSerine 199/202 - 3256030	3256030
RABBIT ANTI-Tau phosphoSerine 199/202 - 3317855	3317855
RABBIT ANTI-Tau phosphoSerine 199/202 - 3417919	3417919
RABBIT ANTI-Tau phosphoSerine 199/202 - 3542494	3542494
RABBIT ANTI-Tau phosphoSerine 199/202 - 3724702	3724702
RABBIT ANTI-Tau phosphoSerine 199/202 - 3984606	3984606

References

Reference overview	Pub Med ID
Distribution of tau protein kinase I/glycogen synthase kinase-3beta, phosphatases 2A and 2B, and phosphorylated tau in the developing rat brain. Takahashi, M., et al. Brain Res., 857(1-2):193-206 (2000) 1999	10700568
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) 1999	10702411
Modulation of tau phosphorylation and intracellular localization by cellular stress. Jenkins, S.M., et al. Biochem. J., 345:263-270 (2000) 1999	10620503
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) 1999	10681533
Regulation of expression, phosphorylation and biological activity of tau during differentiation in SY5Y cells. Haque, N., et al. Brain Res., 838(1-2):69-77 (1999) 1998	10446318
Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies. Sontag, E., et al. J. Biol. Chem., 274:25490-25498 (1999) 1998	10464280
Inhibition of tau phosphorylating protein kinase cdk5 prevents beta-amyloid-induced neuronal death. Alvarez, A., et al. FEBS Lett., 459:421-426 (1999) 1998	10526177
The microtubule binding of tau and high molecular weight tau in apoptotic PC12 cells is impaired because of altered phosphorylation. Davis, P.K. and G.V. Johnson J. Biol. Chem., 274(50):35686-35692 (1999) 1998	10585448
Alzheimer's disease. The tangled tale of tau. Mandelkow, E. Nature , 402(6762):588-589 (1999) 1998	10604460

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Title
Research Focus - Volume 2, 2013

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