Vergleich

Tau phospho S199

ArtNr 18-272-197325
Hersteller GENWAY
Menge 0.05 ml
Kategorie
Typ Antibody
Applikationen WB
Specific against other
ECLASS 10.1 32160702
ECLASS 11.0 32160702
UNSPSC 12352203
Alias GWB-1AFEA9
Similar products 18-272-197325
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Genway ID:
GWB-1AFEA9
Isotype:
IgG
Immunogen:
Synthetic peptide (Human) derived from the region of human tau that contains serine 199.
Antigen Species:
Human
Positive Control:
Recombinant human Tau treated with GSK-3 beta; African green monkey kidney (CV-1) cells stably expressing human four repeat tau and SV40 small T antigen to induce specific inhibition of PP2A
Target:
Tau
Localization:
Mostly found in the axons of neurons in the cytosol and in association with plasma membrane components.
Purification Note:
Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated tau. The final product is generated by affinity chromatography using a tau-derived peptide that is phosphorylated at serine 199. Storage
Preservative:
0. 05% Sodium Azide; Constituents: 50% Glycerol PBS 1mg/ml BSA. pH 7. 3
Application Note:
WB: Use at a dilution of 1/1000. Detects a band of approximately 60 kDa. Can be blocked with Tau peptide - phospho S199 (phospho and non-phospho pair) . Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user. Cellular
Localization:
Mostly found in the axons of neurons in the cytosol and in association with plasma membrane components. Tau is a neuronal microtubule-associated protein found predominantly on axons. The function of tau is to promote tubulin polymerisation and stabilise microtubules but it also serves to link certain signalling pathways to the cytoskeleton. 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. Hyperphosphorylation impairs the microtubule binding function of tau resulting in the destabilisation of microtubules in AD brains ultimately leading to the degeneration of the affected neurons. Hyperphosphorylated tau is also found in a range of other central nervous system disorders. Numerous serine / threonine kinases including GSK 3 beta PKA Cdk 5 and casein kinase II can phosphorylate tau.
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 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.
Subunit:
Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated.
Subcellular Location:
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.
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:
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.
Ptm:
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.
Ptm:
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:
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).
Disease:
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.
Disease:
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.
Disease:
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.
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.
Disease:
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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Menge: 0.05 ml
Lieferbar: In stock
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