Description
Key facts
Detection method:Colorimetric,
Sample types:Tissue Extracts, Cell culture media, Heparin Plasma, Citrate plasma, Cell culture supernatant, Serum, Cell Lysate, EDTA Plasma,
Reacts with:Mouse, Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 0.075 ng/mL,
Range:0.313 - 10 ng/mL,
Assay time:1h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)
Product details:
Cleaved Tau ELISA Kit (Human Asp738/Mouse Asp713) (ab269557) is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of Cleaved Tau (Human Asp738/Mouse Asp713) protein in cell culture supernatant, cell lysate, edta plasma, serum, cit plasma, hep plasma, tissue extracts, and cell culture media. It uses our proprietary SimpleStep ELISA® technology. Quantitate Cleaved Tau (Human Asp738/Mouse Asp713) with 0.075 ng/ml sensitivity.
SimpleStep ELISA® technology employs capture antibodies conjugated to an affinity tag that is recognized by the monoclonal antibody used to coat our SimpleStep ELISA® plates. This approach to sandwich ELISA allows the formation of the antibody-analyte sandwich complex in a single step, significantly reducing assay time. See the SimpleStep ELISA® protocol summary in the image section for further details. Our SimpleStep ELISA® technology provides several benefits:
- Single-wash protocol reduces assay time to 90 minutes or less
- High sensitivity, specificity and reproducibility from superior antibodies
- Fully validated in biological samples
- 96-wells plate breakable into 12 x 8 wells strips
A 384-well SimpleStep ELISA® microplate (ab203359) is available to use as an alternative to the 96-well microplate provided with SimpleStep ELISA® kits.
Tau promotes microtubule assembly and stability; it might be involved in the establishment and maintenance of neuronal polarity. The C-terminus of Tau 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. Tau is expressed predominantly in neurons. Human Tau is expressed at least as 9 isoforms. The long PNS-tau isoform is expressed in the peripheral nervous system while the others are expressed in the central nervous system. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Tau is phosphorylated at various serine and threonine residues. Tau phosphorylation impairs the Tau ability to bind microtubules and leads to microtubule depolymerization. Hyperphosphorylated Tau is the major component of paired helical filaments, the building block of neurofibrillary lesions in Alzheimer’s disease (AD) brain. Tau truncation can affect Tau pathologic characteristics, including its ability to acquire AD-related conformations and to assemble into filaments. Amyloid-beta protein can trigger caspase activation and cellular apoptosis. Several activated caspases, including caspase-3, caspase-7, and caspase-8, can cleave Tau at a highly conserved sequence present in all isoforms generating Cleaved Tau with …SSTGSIDMVD sequence at the carboxy terminus. This carboxy terminal Asp corresponds to, for example, Asp738 of human canonical PNS isoform, Asp421 of human Tau-F isoform, or Asp713 of mouse canonical PNS isoform. The cleavage of Tau at this site is an important inducer of Tau polymerization in AD. This kit is designed to detect all Tau isoforms only when cleaved at the above described site.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Tau also known as microtubule-associated protein Tau (MAPT) plays an important role in stabilizing microtubules in neuronal cells. Tau is primarily found in the central nervous system but also exists in peripheral neurons. Human Tau protein comes in six isoforms due to alternative splicing with molecular weights ranging from 48 kDa to 67 kDa. This protein predominantly locates in the axons of neurons where it maintains the stability of microtubule tracks necessary for axonal transport.
Biological function summary
Tau is involved in the assembly and stabilization of microtubules essential for maintaining neuronal structure. It interacts with microtubule-binding domains (MBD) to bind and bundle microtubules facilitating intracellular transport. Tau forms a part of the neuronal cytoskeleton complex working closely with other cytoskeletal proteins to preserve the proper axonal transport and function. Abnormally phosphorylated Tau often termed phospho-Tau disrupts this complex affecting microtubule stability.
Pathways
Tau has critical involvement in several signaling cascades such as the microtubule-binding and transport pathways. Glycogen synthase kinase 3 beta (GSK3β) and cyclin-dependent kinase 5 (CDK5) frequently phosphorylate Tau controlling its interaction with microtubules. Phosphorylated Tau accumulates leading to the formation of neurofibrillary tangles often observed in neurodegenerative conditions. Additionally Tau interacts with GAPDH impacting cellular energy regulation through potential pathway cross-talk involving oxidative stress responses.
Tau is closely associated with Alzheimer's disease and frontotemporal dementia. In Alzheimer's disease hyperphosphorylated Tau aggregates into paired helical filaments forming neurofibrillary tangles while similar aggregates are observed in frontotemporal dementia. In these conditions Tau links to amyloid precursor protein (APP) where misregulated phosphorylation-driven interactions contribute to neurodegeneration. Identifying phospho-Tau and its altered interactions with related proteins aids in understanding and potentially treating these disorders.
