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AG952 Tau-381, recombinant human

Tau-381, recombinant human MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
UniProt Number: P10636 Entrez Gene Number: NM_005910.3, NM_016834.2, NM_016835.2, NM_016841.2
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50 µg  
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Description
Catalogue NumberAG952
Brand Family Chemicon®
Trade Name
  • Chemicon
DescriptionTau-381, recombinant human
OverviewTau-381

MOL. WT.: 39,700 Da

PEPTIDE CONTENT: 50 μg per vial (protein content and concentration determined by BCA protein assays using BSA as standard).

COUNTER ION: Lyophilized in final buffer of 50 mM MES, pH 6.8, 100 mM NaCl and 0.5 mM EGTA.
Product Information
PresentationWhite lyophilized powder. Resuspend in water at a concentration of 1 mg/mL. This will give you a final of 50 mM MES, pH 6.8, 100 mM NaCl and 0.5 mM EGTA.
Quality LevelMQ100
Biological Information
Purity>90% (determined by SDS-PAGE)
Entrez Gene Number
Entrez Gene SummaryThis 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
  • tau
  • FTDP-17
  • MSTD
  • TAU
  • FLJ31424
  • MTBT1
  • PHF-tau
  • DDPAC
  • MGC138549
  • PPND
UniProt Number
UniProt SummaryFUNCTION: 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.
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 ConditionsMaintain lyophilized material at -20ºC for up to 12 months after date of receipt. After reconstitution maintain at -20ºC to -70ºC for up to 2 weeks in undiluted aliquots. Avoid freeze/thaw cycles to avoid aggregation.
Packaging Information
Material Size50 µg
Global Trade Item Number
Catalogue Number GTIN
AG952 04053252331343