Recombinant Human Microtubule-associated protein tau (MAPT) (Active)

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Code CSB-MP013481HU(F8)
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Size $318
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Activity
    Measured by its binding ability in a functional ELISA. Immobilized Human MAPT at 2 μg/ml can bind Anti-MAPT recombinant antibody (CSB-RA013481A1HU), the EC50 is 4.547-6.284 ng/mL. Biological Activity Assay
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU/ug as determined by LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized Human MAPT at 2 μg/ml can bind Anti-MAPT recombinant antibody (CSB-RA013481A1HU), the EC50 is 4.547-6.284 ng/mL.
Target Names
MAPT
Uniprot No.
Alternative Names
(Neurofibrillary tangle protein)(Paired helical filament-tau)(PHF-tau)
Molecular Characterization
Species
Homo sapiens (Human)
Source
Mammalian cell
Expression Region
1-441aa
Target Protein Sequence
MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
Mol. Weight
49.5 kDa
Protein Length
Full Length of Isoform Tau-F
Tag Info
N-terminal 10xHis-tagged
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
Lyophilized from a 0.2 μm filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Basically, we can dispatch the products out in 3-7 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

This Human MAPT recombinant protein was produced in mammalian cell, where the gene sequence encoding Human MAPT (1-441aa) was expressed with the N-terminal 10xHis-tag. The purity of this MAPT protein was greater than 95% by SDS-PAGE. The activity was validated.

Tau protein plays an important role in different stages of tauopathies. Its abnormal phosphorylation leads to defective axonal transport, synaptic loss and neuroinflammation as early signals of neurodegeneration. Tau protein tangles may be the manifestation of advanced disease, causing the loss of normal cell function and leading to the occurrence of the disease. At the same time, tau protein tangles can also shield many proteins with important functions and aggravate neurological damage. The more thorough the research on tau protein, the more helpful it is to understand degenerative neuropathy, and at the same time, it will be helpful for the treatment of this type of disease. Targeting the metabolism and function of tau protein as a drug target may have important implications for the targeted therapy of degenerative neuropathy. In clinical application, tau protein examination is of great value for evaluating AD, CJD, PART, etc.

 

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Target Background

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/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.
Gene References into Functions
  1. genetic manipulation of Sirt3 revealed that amyloid-beta increased levels of total tau acetylated tau through its modulation of Sirt3. PMID: 29574628
  2. Data suggest that both the small heat shock protein HspB1/Hsp27 and the constitutive chaperone Hsc70/HspA8 interact with tau to prevent tau-fibril/amyloid formation. Chaperones from different families play distinct but complementary roles in prevention of tau-fibril/amyloid formation. (HspB1 = heat shock protein family B small member 1; Hsc70 = heat shock protein family A Hsp70) PMID: 29298892
  3. a 2.0-kDa peptide which biochemically and immunologically resembles the injected amino terminal tau 26-44 was endogenously detected in vivo, being present in hippocampal synaptosomal preparations from Alzheimer's disease subjects. PMID: 29508283
  4. Study reports the identification of new bona fide human brain circular RNAs produced from the MAPT locus. PMID: 29729314
  5. TAU attaches to brain lipid membranes where it self-assembles in a cation-dependent manner. PMID: 29644863
  6. Microtubule hyperacetylation enhances KL1-dependent micronucleation under a Tau deficiency in mammary epithelial cells. PMID: 30142893
  7. This article presents key studies of tau in oligodendrocytes and select important studies of tau in neurons. The extensive work on tau in neurons has considerably advanced the understanding of how tau promotes either health or disease. [review] PMID: 30111714
  8. Zn2 + enhances Tau aggregation-induced apoptosis and toxicity in neuronal cells. PMID: 27890528
  9. Tau binds to synaptic vesicles via its N-terminal domain and interferes with presynaptic functions. PMID: 28492240
  10. Study identifies a potential "two-hit" mechanism in which tau acetylation disengages tau from microtubules (MT) and also promotes tau aggregation. Thus, therapeutic approaches to limit tau K280/K281 acetylation could simultaneously restore MT stability and ameliorate tau pathology in Alzheimer's disease and related tauopathies. PMID: 28287136
  11. In vitro neuroprotective effects of naringenin nanoemulsion against beta-amyloid toxicity through the regulation of amyloidogenesis and tau phosphorylation. PMID: 30001606
  12. To confirm the neuroprotective role of 24-OH, in vivo experiments were run on mice that express human tau without spontaneously developing tau pathology (hTau mice), by means of the intracerebroventricular injection of 24-OH. PMID: 29883958
  13. These findings suggest a relative homogeneous clinicopathological phenotype in P301L MAPT mutation carriers in our series. This phenotype might help in the differential diagnosis from other tauopathies and be a morphological hint for genetic testing. The haplotype analysis results suggest a founder effect of the P301L mutation in this area. PMID: 28934750
  14. Report that the interaction of Tau with vesicles results in the formation of highly stable protein/phospholipid complexes. These complexes are toxic to primary hippocampal cultures and are detected by MC-1, an antibody recognizing pathological Tau conformations. The core of these complexes is comprised of the PHF6* and PHF6 hexapeptide motifs, the latter in a beta-strand conformation. PMID: 29162800
  15. more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS than in FTLD-tau PMID: 28984110
  16. Our data show that the hyperacetylation of Tau by p300 histone acetyltransferase (HAT) disfavors liquid-liquid phase separation , inhibits heparin-induced aggregation, and impedes access to LLPS-initiated microtubule assembly PMID: 29734651
  17. Because neurofibrillary tangles are aberrant intracellular inclusions formed in the AD patients by hyperphosphorylated tau, it was initially proposed that phosphorylated and/or aggregated intracellular tau protein was causative of neuronal death. However, recent studies suggest a toxic role for non-phosphorylated and non-aggregated tau when it is located in the brain extracellular space. [review] PMID: 29584657
  18. MAPT rs242557G/A genetic polymorphism is associated with susceptibility to sporadic AD, and individuals with a GG genotype of rs242557G/A might be at a lower risk. PMID: 29098924
  19. Study indicates that there are at least two common patterns of TDP-43 and tau protein misfolding in human brain aging. In patients lacking substantial Alzheimer's disease pathology, cerebral age-related TDP-43 with sclerosis (CARTS) cases tend to have tau neurofibrillary tangles in the hippocampal dentate granule neurons, providing a potential proxy indicator of CARTS. PMID: 28281308
  20. Patients with Kii amyotrophic lateral sclerosis and parkinsonism-dementia complex (Kii ALS/PDC) had dislocated, multinucleated Purkinje cells and various tau pathologies in the cerebellum. These cerebellar abnormalities may provide new insights into the pathomechanism of Kii ALS/PDC and may provide a neuropathological marker for the condition. PMID: 28236345
  21. The studies findings indicate that p.E372G is a pathogenic microtubule-associated protein tau mutation that causes microtubule-associated protein tau similar to p.G389R. PMID: 27529406
  22. Solven ionic strength, temperature and polarity altered tau conformation dynamics. PMID: 29630971
  23. MAPT alternative splicing is associated with Neurodegenerative Diseases. PMID: 29634760
  24. High tau expression is associated with blood vessel abnormalities and angiogenesis in Alzheimer's disease. PMID: 29358399
  25. We identified common splice factors hnRNP F and hnRNP Q regulating the haplotype-specific splicing of MAPT exon 3 through intronic variants rs1800547 and rs17651213 PMID: 29084565
  26. Cognitive impairment in progressive supranuclear palsy is associated with severity of progressive supranuclear palsy-related tau pathology. PMID: 29082658
  27. These observations indicate the ability of QUE to decrease tau protein hyperphosphorylation and thereby attenuate the associated neuropathology... these results support the potential of QUE as a therapeutic agent for AD and other neurodegenerative tauopathies. PMID: 29207020
  28. Increasing microtubule acetylation rescues human tau-induced microtubule defects and neuromuscular junction abnormalities in Drosophila. PMID: 28819043
  29. The findings reveal the ability of Bin1 to modify actin dynamics and provide a possible mechanistic connection between Bin1 and tau-induced pathobiological changes of the actin cytoskeleton. PMID: 28893863
  30. We find that both the generation of Abeta and the responsiveness of TAU to A-beta are affected by neuronal cell type, with rostral neurons being more sensitive than caudal neurons. PMID: 29153990
  31. The results of the current study indicate that variations in microtubule-associated protein tau influence cognition in progressive supranuclear palsy. PMID: 29076559
  32. The identification of mutations in MAPT, the gene that encodes tau, causing dementia and parkinsonism established the notion that tau aggregation is responsible for the development of disease. PMID: 28789904
  33. CSF tau proteins and their index differentiated between Alzheimer's disease or other dementia patients and cognitively normal subjects, while CSF levels of neurofilaments expressed as their index seem to contribute to the discrimination between patients with neuroinflammation and normal controls or AD patients PMID: 28947837
  34. Comparison of the distributions of tau pTyr18 and double-phosphorylated Syk in the transgenic mouse brain and human hippocampus showed that the phosphorylation of tyrosine 18 in tau already occurs at an early stage of tauopathy and increases with the progression of neurodegeneration. Syk appears unlikely to be a major kinase that phosphorylates tyrosine 18 of tau at the early stage of tauopathy. PMID: 28919467
  35. Study confirmed that Western diet did not exacerbate tau pathology in hTau mice, observed that voluntary treadmill exercise attenuates tau phosphorylation, and reported that caloric restriction seems to exacerbate tau aggregation compared to control and obese hTau mice. PMID: 28779908
  36. Study showed a gradual accumulation of nuclear tau in human cells during aging and its general co-localization with the DAPI-positive heterochromatin, which seems to be related to aging pathologies (neurodegenerative or cancerous diseases), where nuclear AT100 decreases drastically, a condition very evident in the more severe stages of the diseases. PMID: 28974363
  37. Methamphetamine can impair the endoplasmic reticulum-associated degradation pathway and induce neuronal apoptosis through endoplasmic reticulum stress, which is mainly mediated by abnormal CDK5-regulated Tau phosphorylation. PMID: 29705343
  38. Aha1 colocalized with tau pathology in brain tissue, and this association positively correlated with Alzheimer disease progression. PMID: 28827321
  39. Assessed the subcellular localization of tau45-230 fragment using tau45-230-GFP-transfected hippocampal neurons as well as neurons in which this fragment was endogenously generated under experimental conditions that induced neurodegeneration. Results suggested that tau45-230 could exert its toxic effects by partially blocking axonal transport along microtubules, contributing to the early pathology of Alzheimer's disease. PMID: 28844006
  40. frontotemporal dementia and parkinsonism linked to chromosome 17 tau with a mutation in the C-terminal region had different banding patterns, indicating a different phosphorylation pattern. PMID: 27641626
  41. Study demonstrated the presence of the smaller Tau isoform (352 amino acids), whose amount increases in differentiated SK-N-BE cells, with Tau-1/AT8 nuclear distribution related to the differentiation process. PMID: 29684490
  42. In primary-culture fetal astrocytes, streptozotocin increases phosphorylation of Tau at Ser396. alpha-boswellic acid reduced hyperphosphorylated tau (Ser404). Interruption in astroglial Reelin/Akt/Tau signaling pathways may have a role in Alzheimer disease. PMID: 27567921
  43. Screening of MAPT, GRN and CHCHD10 genes in Chinese patients with frontotemporal dementia (FTD) identified about 4.9% mutation carriers. Among the known FTD causative genes tested, MAPT and CHCHD10 play the most important roles in Chinese patients with sporadic FTD. PMID: 28462717
  44. Data show that aggregation of the Tau protein correlates with destabilization of the turn-like structure defined by phosphorylation of Ser202/Thr205. PMID: 28784767
  45. deletion or inhibition of the cytoplasmic shuttling factor HDAC6 suppressed neuritic tau bead formation in neurons. PMID: 28854366
  46. We propose that the H2 haplotype, which expresses reduced 4R tau compared with the H1 haplotype, may exert a protective effect as it allows for more fluid mitochondrial movement along axons with high energy requirements, such as the dopaminergic neurons that degenerate in PD. PMID: 28689993
  47. Results find that overexpression of hTau increases intracellular calcium, which in turn activates calpain-2 and induces degradation of alpha4 nAChR. PMID: 27277673
  48. when misfolded tau assemblies enter the cell, they can be detected and neutralized via a danger response mediated by tau-associated antibodies and the cytosolic Fc receptor tripartite motif protein 21 (TRIM21) PMID: 28049840
  49. stress granules and TIA-1 play a central role in the cell-to-cell transmission of Tau pathology. PMID: 27460788
  50. clinicopathologic study shows inter- and intra-familial clinicopathologic heterogeneity of FTDP-17 due to MAPT p.P301L mutation, including globular glial tauopathy in one patient. PMID: 27859539

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Involvement in disease
Frontotemporal dementia (FTD); Pick disease of the brain (PIDB); Progressive supranuclear palsy 1 (PSNP1); Parkinson-dementia syndrome (PARDE)
Subcellular Location
Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, axon. Cell projection, dendrite. Secreted.
Tissue Specificity
Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.
Database Links

HGNC: 6893

OMIM: 157140

KEGG: hsa:4137

STRING: 9606.ENSP00000340820

UniGene: Hs.101174

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