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AB316703

Recombinant Cleaved Tau Protein Standard

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Recombinant Cleaved Tau Protein Standard is a Mouse Fragment protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.

View Alternative Names

Mtapt, Tau, Mapt, Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau

2 Images
Sandwich ELISA - Recombinant Cleaved Tau Protein Standard (AB316703)
  • sELISA

Supplier Data

Sandwich ELISA - Recombinant Cleaved Tau Protein Standard (AB316703)

Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.

SDS-PAGE - Recombinant Cleaved Tau Protein Standard (AB316703)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Cleaved Tau Protein Standard (AB316703)

SDS-PAGE analysis of ab316703 under reducing conditions for 2ug protein.

Key facts

Purity

>80% SDS-PAGE

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE, sELISA

applications

Biologically active

No

Accession

P10637

Animal free

Yes

Carrier free

No

Species

Mouse

Storage buffer

pH: 7.3 - 7.5 Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.

Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.

The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

Sequence info

[{"sequence":null,"proteinLength":"Fragment","predictedMolecularWeight":"32.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P10637","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

Specifications

Form

Liquid

General info

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.

Post-translational modifications

Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity).. Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in mitosis), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3, MARK4), causing detachment from microtubules, and their disassembly (By similarity). Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C. Phosphorylation at Ser-554 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylation at Ser-188 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons (By similarity).

Subcellular localisation

Cytoskeleton

Product protocols

Target data

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.
See full target information Mapt

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