Abcam, ab318936, Human Tau (phospho T217) ELISA Kit - Extracellular

Size: 1 x 96Tests / 1 x 384Tests / 10 x 96Tests
Human Tau (phospho T217) ELISA Kit - Extracellular is a single-wash 90-min Simplestep used to quantify Human Tau (phospho T217) with a sensitivity of 0.136 ng/mL. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step. - Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader - Different formats for different needs: 10x96 plates for bulk orders and 384-well plate for higher throughput - Validated on a number of sample types including cerebrospinal fluid (CSF)
Key facts
Detection method:Colorimetric,
Sample types:Serum, Citrate plasma, EDTA Plasma, Heparin Plasma, Cell culture supernatant, Cerebral Spinal Fluid,
Reacts with:Human, Mouse, Rat,
Assay type:Sandwich (quantitative),
Sensitivity:= 0.136 ng/mL,
Range:0.469 - 30 ng/mL,
Assay time:1h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
Human Tau (phospho T217) SimpleStep ELISA® kit is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of Tau (phospho T217) protein in Serum, Cit Plasma, EDTA Plasma, Hep Plasma, Cell culture supernatant, Cerebral Spinal Fluid. Quantitate Human Tau (phospho T217) with 0.136 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, available in 10-pack (10 x 96-well plates)
-Also available in a fully validated 384-well format.

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.