Recombinant Human Tau383 protein is a Human Full Length protein, in the 1 to 383 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, WB.
Images
Key facts
- Purity
- >90% Densitometry
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, WB
- Biologically active
- No
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
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
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Recombinant Human Tau383 protein is a Human Full Length protein, in the 1 to 383 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, WB.
Key facts
- Purity
- >90% Densitometry
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, WB
- Biologically active
- No
- Accession
- P10636-6
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00174% PMSF
Sequence info
Amino acid sequence
- Accession
- P10636
- Protein length
- Full Length
- Amino acids
- 1 to 383
- 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
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Tau383 also known as Microtubule-associated protein tau isoform 383 is a protein with a molecular mass of approximately 45 kDa. It plays an important role in stabilizing microtubules which are components of the cytoskeleton essential for maintaining cell structure and facilitating intracellular transport. Tau383 is characterized by its ability to bind to and promote the polymerization of tubulin into microtubules. It is predominantly expressed in neurons particularly in axons where it regulates the dynamic stability of microtubules essential for efficient neuronal function.
- Biological function summary
Tau383 contributes to cellular processes related to the maintenance of neuronal structure and function. It acts as a microtubule-associated protein within the axonal cytoskeleton network. This protein does not typically form complexes but its interaction with microtubules is important for their assembly and stabilization. Alterations in its expression or post-translational modifications can significantly impact microtubule function and neuronal health.
- Pathways
Tau383 plays an important role in the microtubule regulation pathways that are vital for axonal transport and cytoskeletal dynamics. It is closely associated with kinases and phosphatases such as glycogen synthase kinase 3 beta (GSK3β) and protein phosphatase 2A (PP2A) which regulate its phosphorylation state. The phosphorylation of Tau383 affects its ability to bind to microtubules influencing the pathways that are fundamental for synaptic plasticity and neuronal development.
- Associated diseases and disorders
Tau383 is particularly implicated in neurodegenerative conditions such as Alzheimer's disease and frontotemporal dementia. Abnormal hyperphosphorylation of Tau383 leads to the formation of neurofibrillary tangles a hallmark of Alzheimer's pathology. This process involves altered interactions with proteins like amyloid-beta whereby Tau383 aggregation exacerbates neuronal damage and cognitive decline in these disorders. Consequently Tau383 is a significant target for therapeutic interventions aiming to alleviate tau-related pathologies in neurodegenerative diseases.
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1 product image
SDS-PAGE - Recombinant Human Tau383 protein (ab84766)
SDS-PAGE showing ab84766 at approximately 52kDa.
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