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AB241263

Recombinant Mouse Tau protein (His tag)

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Recombinant Mouse Tau protein (His tag) is a Mouse Full Length protein, in the 2 to 733 aa range, expressed in Yeast, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

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

3 Images
Mass Spectrometry - Recombinant Mouse Tau protein (His tag) (AB241263)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Mouse Tau protein (His tag) (AB241263)

Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of ab241263 could indicate that this peptide derived from Yeast-expressed Mus musculus (Mouse) Mapt.

Mass Spectrometry - Recombinant Mouse Tau protein (His tag) (AB241263)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Mouse Tau protein (His tag) (AB241263)

Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of ab241263 could indicate that this peptide derived from Yeast-expressed Mus musculus (Mouse) Mapt.

SDS-PAGE - Recombinant Mouse Tau protein (His tag) (AB241263)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Mouse Tau protein (His tag) (AB241263)

Analysis of ab241263 by (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Key facts

Purity

>90% SDS-PAGE

Expression system

Yeast

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P10637

Animal free

No

Carrier free

No

Species

Mouse

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"ADPRQEFDTMEDHAGDYTLLQDQEGDMDHGLKESPPQPPADDGAEEPGSETSDAKSTPTAEDVTAPLVDERAPDKQAAAQPHTEIPEGITAEEAGIGDTPNQEDQAAGHVTQGRREGQAPDLGTSDWTRQQVSSMSGAPLLPQGLREATCQPSGTRPEDIEKSHPASELLRRGPPQKEGWGQDRLGSEEEVDEDLTVDESSQDSPPSQASLTPGRAAPQAGSGSVCGETASVPGLPTEGSVPLPADFFSKVSAETQASQPEGPGTGPMEEGHEAAPEFTFHVEIKASTPKEQDLEGATVVGVPGEEQKAQTQGPSVGKGTKEASLQEPPGKQPAAGLPGRPVSRVPQLKARVASKDRTGNDEKKAKTSTPSCAKAPSHRPCLSPTRPTLGSSDPLIKPSSPAVSPEPATSPKHVSSVTPRNGSPGTKQMKLKGADGKTGAKIATPRGAASPAQKGTSNATRIPAKTTPSPKTPPGSGEPPKSGERSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSASKSRLQTAPVPMPDLKNVRSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL","proteinLength":"Full Length","predictedMolecularWeight":"78.1 kDa","actualMolecularWeight":null,"aminoAcidEnd":733,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Yeast","accessionNumber":"P10637","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
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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