Recombinant Mouse Microtubule-associated protein tau (Mapt) (Active)

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中文名稱：

小鼠Mapt重組蛋白
貨號：

CSB-MP013481MO
說明書：

MSDS Datasheet
規(guī)格：

￥828
圖片：
(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 Mouse Mapt at 2 μg/ml can bind anti-MAPT recombinant antibody (CSB-RA013481A1HU),the EC₅₀ is 436.1-518.6 ng/mL. Biological Activity Assay
其他：

產(chǎn)品詳情
產(chǎn)品評價(jià)
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

純度：

Greater than 90% as determined by SDS-PAGE.
內(nèi)毒素：

Less than 1.0 EU/ug as determined by LAL method.
生物活性：

Measured by its binding ability in a functional ELISA. Immobilized Mouse Mapt at 2 μg/mL can bind anti-MAPT recombinant antibody (CSB-RA013481A1HU),the EC₅₀ is 436.1-518.6 ng/mL.
基因名：

Mapt
Uniprot No.：

P10637
別名：

(Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)
分子結(jié)構(gòu)：
種屬：

Mus musculus (Mouse)
蛋白長度：

Full Length of Mature Protein
來源：

Mammalian cell
分子量：

78.9 kDa
表達(dá)區(qū)域：

2-733aa
氨基酸序列

ADPRQEFDTMEDHAGDYTLLQDQEGDMDHGLKESPPQPPADDGAEEPGSETSDAKSTPTAEDVTAPLVDERAPDKQAAAQPHTEIPEGITAEEAGIGDTPNQEDQAAGHVTQGRREGQAPDLGTSDWTRQQVSSMSGAPLLPQGLREATCQPSGTRPEDIEKSHPASELLRRGPPQKEGWGQDRLGSEEEVDEDLTVDESSQDSPPSQASLTPGRAAPQAGSGSVCGETASVPGLPTEGSVPLPADFFSKVSAETQASQPEGPGTGPMEEGHEAAPEFTFHVEIKASTPKEQDLEGATVVGVPGEEQKAQTQGPSVGKGTKEASLQEPPGKQPAAGLPGRPVSRVPQLKARVASKDRTGNDEKKAKTSTPSCAKAPSHRPCLSPTRPTLGSSDPLIKPSSPAVSPEPATSPKHVSSVTPRNGSPGTKQMKLKGADGKTGAKIATPRGAASPAQKGTSNATRIPAKTTPSPKTPPGSGEPPKSGERSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSASKSRLQTAPVPMPDLKNVRSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
蛋白標(biāo)簽：

N-terminal 10xHis-tagged
產(chǎn)品提供形式：

Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
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.
緩沖液：

Lyophilized from a 0.2 μm filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
復(fù)溶：

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.
儲(chǔ)存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)期：

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.
貨期：

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.
注意事項(xiàng)：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
產(chǎn)品描述：

The gene corresponding to the 2-733aa off the mouse microtubule-associated protein tau (MAPT) was fused with the 10xHis-tagged at the N-terminus and then cloned into a plasmid vector, forming the recombinant vector. Mammalian cells were transfected with the recombinant vector, allowing for its expression. The product was purified to obtain the N-terminal 10xHis-tagged recombinant mouse MAPT protein. Its purity is greater than 92% determined by SDS-PAGE. The endotoxin of this protein is less than 1.0 EU/ug measured by the LAL method. Its activity has also been validated through a functional ELISA. This MAPT protein can bind the anti-MAPT recombinant antibody, with the EC₅₀ of 436.1-518.6 ng/mL.

MAPT protein, also called Tau, is abundant in neurons of the central nervous system (CNS), while relatively low in non-neuron cells like astrocytes and oligodendrocytes. Tau is involved in the regulation of axon transport, the maintenance of nuclear function to protect DNA integrity, the interaction with actin cytoskeleton to promote the formation of actin filaments, and the government of NMDA receptor signaling pathway through interaction with Fyn. Since its involvement in numerous neurodegenerative diseases such as Alzheimer's disease (AD) and primary age-related tau lesions (PART), Tau has become a hot target for therapy of these disorders. In clinical application, Tau protein examination is of great value for the evaluation of AD and PART.
Datasheet & COA：

Please contact us to get it.

產(chǎn)品評價(jià)

靶點(diǎn)詳情

功能：

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.
基因功能參考文獻(xiàn)：
1. that tau modulates motility in a motor-specific manner to direct intracellular transport PMID: 29077261
2. the AD-like tau accumulation induces anxiety through disrupting miR92a-vGAT-GABA signaling, which reveals molecular mechanisms underlying the anxiety behavior in AD patients and potentially leads to the development of new therapeutics for tauopathies. PMID: 28129110
3. These results show for the first time that the phosphorylation and isoform alteration of tau are regulated differently during mouse development. PMID: 29196605
4. In adult and aged tau(+/+), tau(+/-), tau(-/-) mice tau deficiency could not induce significant motor disorders. However, found lower expression levels of transcription factors Orthodenticle homeobox 2 (OTX2) of midbrain dopaminergic neurons in older aged mice. Results suggested that tau deficiency alone might not be enough to mimic the pathology of Parkinson's disease. PMID: 29337233
5. Tau deletion increased ATP production and improved the recognition memory and attentive capacity of juvenile mice. PMID: 30077079
6. MAPT variant interaction with mutant amyloid protein precursor causes frontotemporal dementia. PMID: 29729423
7. These results establish that in addition to the neuritic plaque, a second determinant is required to drive the conversion of wild-type tau. PMID: 27373369
8. miR-322 promotes Tau phosphorylation via negatively controlling BDNF-TrkB receptor activation PMID: 29464486
9. High tau expression is associated with blood vessel abnormalities and angiogenesis in Alzheimer's disease. PMID: 29358399
10. Disinhibiation of Gas6 binding to Tyro3 due to PGRN reduction results in activation of PKCalpha via PLCgamma, inducing tau phosphorylation at Ser203, mislocalization of tau to dendritic spines, and spine loss. PMID: 29382817
11. 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
12. For the three conditions, FRAP analysis revealed a similar mobility in dendrites compared with axons; however, Tau-mEOS2 was less mobile than hWT-Tau and hP301L-Tau and the mobile fraction was smaller, possibly reflecting less efficient microtubule binding of Tau when over-expressed. Together, our study presents Tau-mEOS2 mice as a novel tool for the study of Tau in a physiological and a pathological context. PMID: 27378256
13. Chronic Dyrk1 inhibition reversed cognitive deficits in Alzheimer's disease transgenic mice via reduction of APP and phosphorylated tau pathology. PMID: 28779511
14. Results suggest the importance of the autophagosome for the low-frequency stimulation-induced oligomerization of tau and suggest a reason for its age dependency. Interestingly, the lysosomal disturbance promoted the formation of the fibrillar form of aggregates consisting of hyper-phosphorylated tau. PMID: 28874186
15. deletion or inhibition of the cytoplasmic shuttling factor HDAC6 suppressed neuritic tau bead formation in neurons. PMID: 28854366
16. The present findings support the idea that the progressive accumulation of phospho-tau is associated with structural alterations of the GA, and that these changes may occur in the absence of Abeta pathology. PMID: 28922155
17. MicroRNA-146a suppresses ROCK1 allowing hyperphosphorylation of tau in Alzheimer's disease. PMID: 27221467
18. results demonstrate that ApoE affects tau pathogenesis, neuroinflammation, and tau-mediated neurodegeneration independently of amyloid-beta pathology; ApoE4 exerts a 'toxic' gain of function whereas the absence of ApoE is protective PMID: 28959956
19. Study demonstrated that, in ob/ob mice, type 2 diabetes leads to a progressive tau hyperphosphorylation due to hypothermia, which is reversed by normothermia but not by acute leptin injections or 15 weeks caffeine treatment. PMID: 27793638
20. study reports that tau is present in the heart and loss of tau in the heart causes elevated blood pressure and altered cardiac performance in aged mice. PMID: 28059795
21. These data are consistent with other observations that the rapidly depositing Tg4510 mouse is a challenging model in which to demonstrate efficacy of tau-lowering treatments compared to some other preclinical models of tau deposition/overexpression. PMID: 28655349
22. Data show that tau promotes excitotoxicity by a post-synaptic mechanism. PMID: 28883427
23. Tau as an essential mediator of the adverse effects of stress on brain structure and function. PMID: 27274066
24. Study demonstrated that phosphorylated-tau spreads gradually and selectively from the injured cortex to other brain regions after traumatic brain injury and that all of the affected regions are part of the working memory circuit. PMID: 28163095
25. Study demonstrates a mechanistic link between brain Abeta deposition and CSF tau, and thus, CSF tau may present an important readout of Abeta deposition in mouse models and likely in Alzheimer's disease. PMID: 27750032
26. Tau efflux from the brain to the blood was evaluated by administering radioactively labeled and unlabeled tau intracerebroventricularly in wild-type and tau knock-out mice, respectively. The efflux of Tau, including a fraction via CNS-derived L1CAM exosomes, was observed in mice. Tau is readily transported from the brain to the blood. PMID: 27234211
27. Somatodendritic accumulation of Tau in Alzheimer's disease is promoted by Fyn-mediated local protein translation. PMID: 28864542
28. Intermittent hypoxia treatment (IHT)-induced cognitive impairment may be partially explained by the fact that IHT increases phosphorylated tau via biological processes common to aging. PMID: 28057021
29. Pin1 serves as a positive regulatory molecule of proplatelet formation of megakaryocytes by enhancing the function of phosphorylated tau. PMID: 28943044
30. PGRN decrease, resulting from pathogenic mutations, might compromise the trophism of cortical neurons by affecting GluN2B-contaning NMDA receptors PMID: 28899992
31. These data provide evidence that amyloid beta acts to enhance tau pathology by increasing the formation of tau species capable of seeding new aggregates. PMID: 28500862
32. These results suggest that tau haploinsufficiency, without the compensation effect of MAP1A, induces reduction of Otx2 expression, increases prenatal cell death, and accordingly leads to selective loss of VTA DA neurons in the early postnatal stage. PMID: 28424350
33. High-glucose induces tau hyperphosphorylation through activation of TLR9-P38 MAPK pathway. PMID: 28803064
34. these results uncover a novel role for mDia1 in Abeta-mediated synaptotoxicity and demonstrate that inhibition of MT dynamics and accumulation of PTMs are driving factors for the induction of tau-mediated neuronal damage. PMID: 28877993
35. The authors show here that miR-132 loss exacerbates both amyloid and TAU pathology via inositol 1,4,5-trisphosphate 3-kinase B (ITPKB) upregulation in an Alzheimer's disease mouse model. PMID: 27485122
36. TIA1 knockdown or knockout inhibits tau misfolding and associated toxicity in cultured hippocampal neurons, while overexpressing TIA1 induces tau misfolding and stimulates neurodegeneration. PMID: 27160897
37. Data suggest that a switch in post-translational processing of Tau from acetylation at Lys321 to phosphorylation at Ser324 coordinately regulates Tau aggregation and may be relevant in tauopathy and Alzheimer disease; acetylation/phosphorylation of Tau appears to be controlled by Hdac6 (histone deacetylase 6 protein). PMID: 28760828
38. ROS produced by 1,2-diacetylbenzene causes tau hyperphosphorylation via GSK-3beta phosphorylation and it might be related to impaired memory deficit. PMID: 28734998
39. tau overexpression mediates the excitatory toxicity induced by E-NMDAR activation through inhibiting ERK phosphorylation. PMID: 27809304
40. Data suggest that a presumed diffusion barrier within axon initial segment (AIS) regulates wild-type Tau sorting: retrograde (axon-to-soma) and anterograde (soma-to-axon) sorting of Tau. Tau isoforms without N-terminal inserts are sorted efficiently into axons; a longer isoform (2N4R-Tau) is partially retained in cell bodies/dendrites and accelerates spine/dendrite growth. PMID: 28536263
41. This study establishes a mouse model of sporadic tauopathies and points to important differences between tau fibrils that are generated artificially and authentic ones that develop in Alzheimer's disease brains. PMID: 27810929
42. tau diffusion on microtubules enables to keep microtubules evenly distributed in axonal sections at low tau levels. PMID: 27076215
43. Upregulating HSF1 relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP and increasing HSP70 a5 (BiP/GRP78). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 being one likely key player in both systems. PMID: 28678786
44. our findings suggest that tau is a common downstream factor in both amyloid-dependent and-independent pathogenic mechanisms and therefore could be a more effective drug target for therapeutic intervention in AD. PMID: 27459671
45. Study focused functional consequences of human tau accumulation: aging htau mice (deficient of murine tau but express all six human tau isoforms) compared with murine tau knock-out and C57Bl/6J mice; reduced food-burrowing performance was the most robust aspect of the htau phenotype with aging, htau phenotype appeared stronger than the mtau(-/-) phenotype at young ages but milder with aging. PMID: 27167086
46. Results may provide support for the hypothesis that enhanced expression of tau following lipopolysaccharide administration is a protective measure by hippocampal neurons to compensate for the loss of the microtubule-stabilizing protein due to phosphorylation. More importantly, our results support the hypothesis that blocking the production of Abeta that follows inflammation also leads to reduced tau phosphorylation PMID: 27320209
47. Study identified microtubule-associated protein tau as a highly sensitive constituent of the cytoskeleton in the presence of experimental stroke, thus providing novel evidence for a pivotal role of cytoskeletal elements under ischemic conditions PMID: 27189884
48. These findings suggest that TDP-43 promotes tau exon 10 inclusion and 4R-tau expression and that disease-related changes of TDP-43, truncations and mutations, affect its function in tau exon 10 splicing, possibly because of TDP-43 mislocalization to the cytoplasm. PMID: 28487370
49. Thus, these data demonstrate that Tau(-/-) mice show impairments in the maturation of newborn granule neurons under basal conditions and that they are insensitive to the modulation of adult hippocampal neurogenesis exerted by both stimulatory and detrimental stimuli. PMID: 27198172
50. this work provides insights into postsynaptic processes in Alzheimer's disease pathogenesis and challenges a purely pathogenic role of tau phosphorylation in neuronal toxicity. PMID: 27856911
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相關(guān)疾病：

May be involved in the pathogenesis of cytoplasmic inclusions (as Mallory bodies) in livers of mice chronically intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-dihydrocollidine), a model for human alcoholic hepatitis. Alteration of Tau (abnormal phosphorylation and cross-linking) could contribute to Mallory bodies formation and disturbance of microtubule function in alcoholic liver disease.
亞細(xì)胞定位：

Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, axon. Cell projection, dendrite. Secreted.
組織特異性：

Expressed in neurons and at a lower level in the liver and kidney. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.
數(shù)據(jù)庫鏈接：

KEGG: mmu:17762

STRING: 10090.ENSMUSP00000097919

UniGene: Mm.1287