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ABN1703

Sigma-Aldrich

Anti-Tau, AEP-cleaved (N368) Antibody

serum, from rabbit

Sinónimos:

Microtubule-associated protein tau, AEP-cleaved N368 fragment, Neurofibrillary tangle protein, AEP-cleaved N368 fragment, Paired helical filament-tau, AEP-cleaved N368 fragment, PHF-tau, AEP-cleaved N368 fragment, Tau, AEP-cleaved N368 fragment

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

species reactivity (predicted by homology)

canine (based on 100% sequence homology), mouse (based on 100% sequence homology), rat (based on 100% sequence homology), monkey (based on 100% sequence homology), bovine (based on 100% sequence homology)

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

dog ... Mapt(480488)
human ... MAPT(4137)
mouse ... Mapt(17762) , Mapt(281296)
rat ... Mapt(29477)
rhesus monkey ... Mapt(574327)

General description

Microtubule-associated protein Tau (UniProt P10636; also known as Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau) is encoded by the MAPT (also known as TAU, MAPT1, MTBTL) gene (Gene ID 4137) in human. Neurofibrillary tangles (NFTs), composed of truncated and hyperphosphorylated Tau, are a common feature of aging-related neurodegenerative diseases, including Alzheimer′s disease (AD). In addition to caspases-mediated cleavage at Asp421, Tau can also be cleaved at Asn255 and Asn368 by the lysosomal cysteine proteinase asparagine endopeptidase (AEP). AEP is upregulated in aged brain, as well as n human AD brain and tau P301S–transgenic mice with synaptic pathology and behavioral impairments. AEP-mediated tau cleavage abolishes tau microtubule assembly function, induces tau aggregation and triggers neurodegeneration. AEP knockout or functional blockage in tau P301S mice leads to a reduction of tau hyperphosphorylation, protection against memory loss, and a reduction in tau P301S–triggered pathological and behavioral defects.

Specificity

Specifically recognizes AEP-generated Tau fragments with N368 as the c-termus. Does not react with full-length Tau or Tau fragments with other cleaved c-termus. Uniprot P10636 lists 9 human tau isoforms produced by alternative splicing. The N368 designation was originally assigned to this polyclonal antiserum based on Asp368 of isoform 8 (Tau-F, Tau-4), which is equivalent to N685 of isoform 1 (PNS-tau), N279 of isoform 2 (Fetal-tau), N243 of isoform 3 (Tau-A), N308 of isoform 4 (Tau-B), N337 of isoform 5 (Tau-C, Tau-3), N310 of isoform 6 (Tau-D), N339 of isoform 7 (Tau-E), and N703 of isoform 9 (Tau-G).

Immunogen

Epitope: C-terminus
KLH-conjugated linear peptide corresponding to the C-terminal end sequence of AEP-cleaved human Tau N-terminal fragment N368

application

Research Category
Neuroscience
Research Sub Category
Developmental Signaling
This Anti-Tau, AEP-cleaved (N368) Antibody is validated for use in Western Blotting for the detection of AEP-cleaved Tau N-terminal fragment (N368).

Quality

Evaluated by Western Blotting using purified Tau.

Western Blotting Analysis: A 1:100,000 dilution of this antiserum specifically detected 1 µg of purified aa 1-368 Tau fragment, but not the full-length Tau protein.

Target description

~45 kDa observed. Variable depending on the isoform and size of the target fragments.

Physical form

Rabbit polyclonal antiserum with 0.05% sodium azide.
Unpurified

Storage and Stability

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

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.

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Descripción
Precios

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Kerstin Schlegel et al.
Acta neuropathologica communications, 7(1), 177-177 (2019-11-15)
Intraneuronal insoluble inclusions made of Tau protein are neuropathological hallmarks of Alzheimer Disease (AD). Cleavage of Tau by legumain (LGMN) has been proposed to be crucial for aggregation of Tau into fibrils. However, it remains unclear if LGMN-cleaved Tau fragments
Kathy Zhang et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 44(28) (2024-06-04)
Chronic sleep disruption (CSD), from insufficient or fragmented sleep and is an important risk factor for Alzheimer's disease (AD). Underlying mechanisms are not understood. CSD in mice results in degeneration of locus ceruleus neurons (LCn) and CA1 hippocampal neurons and
Qing-Qing Xu et al.
Journal of neuroinflammation, 20(1), 19-19 (2023-02-01)
Alzheimer's disease (AD) is a chronic neurodegenerative disease characterized by progressive cognitive dysfunctions and behavioral impairments. Patchouli alcohol (PA), isolated from Pogostemonis Herba, exhibits multiple pharmacological properties, including neuroprotective effects. This study aimed to investigate the therapeutic effects of PA
Annika Behrendt et al.
Neurobiology of disease, 130, 104518-104518 (2019-06-24)
Tau cleavage by different proteolytic enzymes generates short, aggregation-prone fragments that have been implicated in the pathogenesis of Alzheimer's disease (AD). Asparagine endopeptidase (AEP) activity in particular has been associated with tau dysfunction and aggregation, and the activity of the

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