Recombinant human Tau (mutated P301L) protein (Active) is a Human Fragment protein, in the 558 to 697 aa range with >95% purity and suitable for SDS-PAGE and Functional studies. The predicted molecular weight of ab256151 protein is 15.1 kDa.
- Suitable for Thioflavin T Fluorescence assay
- Save time and ensure accurate results - use our recombinant Tau (mutated P301L) protein as a control
- Optimal protein bioactivity, stability and reproducibility
Images
Key facts
- Purity
- >95%
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Amino acid sequence
S R L Q T A P V P M P D L K N V K S K I G S T E N L K H Q P G G G K V Q I I N K K L D L S N V Q S K C G S K D N I K H V L G G G S V Q I V Y K P V D L S K V T S K C G S L G N I H H K P G G G Q V E V K S E K L D F K D R V Q S K I G S L D N I T H V P G G G N K K I E T H K L T F R E
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Target data
Function
Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). 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 (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT 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.
Alternative names
MAPTL, MTBT1, TAU, MAPT, Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau
Recommended products
Recombinant human Tau (mutated P301L) protein (Active) is a Human Fragment protein, in the 558 to 697 aa range with >95% purity and suitable for SDS-PAGE and Functional studies. The predicted molecular weight of ab256151 protein is 15.1 kDa.
- Suitable for Thioflavin T Fluorescence assay
- Save time and ensure accurate results - use our recombinant Tau (mutated P301L) protein as a control
- Optimal protein bioactivity, stability and reproducibility
Key facts
- Purity
- >95%
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) in tau K18 P301L monomers (ab256151) over time. Thioflavin T ex = 450 nm, em = 485 nm.
- Accession
- P10636-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 7.4
Constituents: 0.58% Sodium chloride, 0.24% HEPES
Sequence info
Amino acid sequence
- S R L Q T A P V P M P D L K N V K S K I G S T E N L K H Q P G G G K V Q I I N K K L D L S N V Q S K C G S K D N I K H V L G G G S V Q I V Y K P V D L S K V T S K C G S L G N I H H K P G G G Q V E V K S E K L D F K D R V Q S K I G S L D N I T H V P G G G N K K I E T H K L T F R E
- Accession
- P10636
- Protein length
- Fragment
- Predicted molecular weight
- 15.1 kDa
- Amino acids
- 558 to 697
- Nature
- Recombinant
Specifications
- Form
- Liquid
General info
- Function
Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). 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 (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT 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
Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3 or MARK4), causing detachment from microtubules, and their disassembly (PubMed:23666762, PubMed:7706316). Phosphorylation decreases with age. Phosphorylation within tau/MAP's repeat domain or in flanking regions seems to reduce tau/MAP's interaction with, respectively, microtubules or plasma membrane components (PubMed:7706316). Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis. Phosphorylation at Ser-548 by GSK3B reduces ability to bind and stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons. There is a reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces glycosylation by a factor of 2 and 4 respectively. Phosphorylation on Ser-721 is reduced by about 41.5% by GlcNAcylation on Ser-717. Dephosphorylated at several serine and threonine residues by the serine/threonine phosphatase PPP5C.
- Subcellular localisation
- Cytoskeleton
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
Protein Monomer.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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.
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2 product images
Functional Studies - Recombinant human Tau (mutated P301L) protein (Active) (ab256151)
Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) in tau K18 P301L monomers (ab256151) over time. Thioflavin T ex = 450 nm, em = 485 nm.
SDS-PAGE - Recombinant human Tau (mutated P301L) protein (Active) (ab256151)
SDS-PAGE - Recombinant human Tau (mutated P301 L) protein (Active) (ab256151).
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