Item no. |
06-785-213091 |
Manufacturer |
GENWAY
|
Amount |
0.1 mg |
Category |
|
Type |
Peptides |
Specific against |
other |
ECLASS 10.1 |
32160409 |
ECLASS 11.0 |
32160409 |
UNSPSC |
12352202 |
Alias |
GWB-F07894 |
Similar products |
06-785-213091 |
Available |
|
Genway ID: |
GWB-F07894 |
Form of Peptide: |
Peptide in 10 mM phosphate buffered saline (without Mg2+ and Ca2+) pH 7. 4 150mM NaCl 0. 1 mM EDTA 1 mg/ml BSA 5% DMF and 5% glycerol. Peptide Information: The synthesized phosphopeptide was derived from human Tau around the phosphorylation site of serine 396 (Y-K-SP-P-V). Quality Control: The quality of the peptide was evaluated by reversed-phase HPLC and mass spectrometry. |
Specificity: |
The peptide specifically blocks the signal of Tau (Phospho-Ser396) antibody completely in Western blotting and IHC. |
Applications: |
For |
Western Blotting: |
add 10 ul of antibody and 10 ul of blocking peptide to 10 ml of antibody dilution buffer and incubate at 4C over night or at room temperature for 2 hours before allowing to react with the blot. |
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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All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.