Phospho-MAPT (T231) Antibody

Code CSB-PA010020
Size US$167
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Product Details

Uniprot No. P10636
Target Names MAPT
Alternative Names AI413597 antibody; AW045860 antibody; DDPAC antibody; FLJ31424 antibody; FTDP 17 antibody; G protein beta1/gamma2 subunit interacting factor 1 antibody; MAPT antibody; MAPTL antibody; MGC134287 antibody; MGC138549 antibody; MGC156663 antibody; Microtubule associated protein tau antibody; Microtubule associated protein tau isoform 4 antibody; Microtubule-associated protein tau antibody; MSTD antibody; Mtapt antibody; MTBT1 antibody; MTBT2 antibody; Neurofibrillary tangle protein antibody; Paired helical filament tau antibody; Paired helical filament-tau antibody; PHF tau antibody; PHF-tau antibody; PPND antibody; PPP1R103 antibody; Protein phosphatase 1, regulatory subunit 103 antibody; pTau antibody; RNPTAU antibody; TAU antibody; TAU_HUMAN antibody; Tauopathy and respiratory failure antibody; Tauopathy and respiratory failure, included antibody
Raised in Rabbit
Species Reactivity Human,Mouse,Rat
Immunogen Synthesized peptide derived from Human Tau around the phosphorylation site of T231.
Immunogen Species Homo sapiens (Human)
Conjugate Non-conjugated
Isotype IgG
Purification Method The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration It differs from different batches. Please contact us to confirm it.
Buffer Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Form Liquid
Tested Applications WB, ELISA
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:2000
ELISA 1:10000
Protocols Western Blotting(WB) Protocol
ELISA Protocol
Troubleshooting and FAQs Antibody FAQs
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Target Data

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
  51. Results show that polyethyleneimine and polypeptide arginine significantly inhibit tau peptides and protein aggregation. The study could be applied to understand tau protein aggregation mechanism in the presence of cationic polymers. PMID: 28456996
  52. Extracts from tauopathy patient samples, which contain four-repeat (4R) tau prions, were transmitted to HEK293 cells expressing 4R tau fused to YFP. These studies demonstrated that prion propagation in HEK cells requires isoform pairing between the infecting prion and the recipient substrate. PMID: 27911827
  53. MicroRNA-146a suppresses ROCK1 allowing hyperphosphorylation of tau in Alzheimer's disease. PMID: 27221467
  54. The authors found that as already shown for oligomeric Abeta, also oligomeric Tau can bind to amyloid precursor protein (APP). Moreover, efficient intra-neuronal uptake of oligomeric Abeta and oligomeric Tau requires expression of APP. PMID: 28696204
  55. MAPT is associated with risk of neurodegenerative diseases, suggesting crucial roles of tau in neurodegenerative processes. PMID: 28402959
  56. Levels of tau correlated with severity and outcome of stroke in both plasma and CSF. PMID: 28854881
  57. 2N4R or 2N3R tau oligomers provoked aggregation of endogenous intracellular tau much more effectively than monomers or fibrils, or of oligomers made from other tau isoforms, and that a mixture of all six isoforms most potently provoked intracellular tau accumulation. These effects were associated with invasion of tau into the somatodendritic compartment. PMID: 28482642
  58. An imbalanced regulation in protein kinases and protein phosphatases is the direct cause of tau hyperphosphorylation in Alzheimer's disease; GSK-3beta and PP2A are the most implicated. (Review) PMID: 28585125
  59. axonal impairment in temporal lobe epilepsy may be mediated by NMDAR via GSK-3beta and Cdk5. In addition, inhibiting either NMDARs or GSK-3beta lowered the relative tau phosphorylation level by reversing the decrease of total tau without affecting phosphorylated tau S396 and T231. PMID: 28595035
  60. Cis phosphorylated tau (cis P-tau) is induced in cortical axons and cerebrospinal fluid and positively correlates with axonal injury and clinical outcome. PMID: 29042562
  61. Tau depletion impairs the survival of CDA-deficient cells by favoring cellular DNA damage and replication stress. PMID: 28947735
  62. A 56-year-old patient suffering from frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17). The history included a three-generation pedigree and the patient was found to be a MAPT mutation carrier. The diagnosis was hindered by late appearance of the hypokinetic movement disorder. PMID: 27905268
  63. This pilot study using lumbar CSF, the p-tau/t-tau ratio, but not t-TDP-43 levels, were significantly different between FTLD-TDP and FTLD-tau patients. PMID: 27662293
  64. These findings of this study demonstrated that reduced bone mineral density occurs earlier than overt degeneration in a tau-based Alzheimer's Disease model and that pathological changes in tau phosphorylation occur in the serotonin-producing neurons of the brainstem raphe in these mice. PMID: 27814296
  65. Study detected high levels of both tau and p-tau in dendritic spine of P301L transgenic mice, a model of tauopathy. p-tau correlated with a significant reduction of post-synaptic makers and its levels are higher in female than in male mice: the increased p-tau was consistent with a proportional decrease in the post-synaptic marker levels analyzed. P301L-tg females showed a more severe synaptopathy compared to males. PMID: 28157099
  66. Study found that found tau proteins cross the blood-brain barrier in both the brain-to-blood and blood-to-brain directions. For Tau-410, studyfound a saturable component for the transport into brain. Study found most tau proteins to be stable in blood and brain and that the tau proteins, especially Tau 121-227, are sequestered by brain. PMID: 27662303
  67. Furthermore, we describe how a variety of transgenic animal strains, each with distinct utility, have been used to identify both genetic and pharmacological modifiers of toxicity in C. elegans. [review] PMID: 29022701
  68. The results indicated that vitamin B12 interacts with tau protein and prevents fibrillization of tau protein. Blocking the cysteine residues of tau confirmed the cysteine-mediated binding of vitamin B12 to tau and showed that binding to cysteine is essential for inhibitory effect of vitamin B12 on tau aggregation. PMID: 28841372
  69. The assay is reproducible across users and works with different commercially available iPSC lines, representing a highly translational tool for the identification of novel treatments against tauopathies, including Alzheimer's disease PMID: 26984927
  70. This study is a reappraisal of the strong association of APOE variability with Alzheimer's dementia in southern India when compared to other dementia groups, while the transcriptional differences between MAPT haplotypes have a limited role in Indian dementia patients. PMID: 27705964
  71. PD patients homozygous for the H1 haplotype have a higher burden of neocortical LB pathology. PMID: 27098667
  72. the tau isoforms with exon-2 and exon-10 segments increase in CSF of sporadic Creutzfeldt-Jakob disease and some types of genetic Creutzfeldt-Jakob disease. PMID: 26188647
  73. Tau protein, along with amyloidBeta42 and GFAP, were increased in plasma up to 90 days after traumatic brain injury compared with controls. PMID: 27312416
  74. In professional ice hockey players, serum levels of Tau-C were significantly higher in post-concussion samples compared with pre-concussive. PMID: 25621407
  75. The development of NFTs within the cholinergic nucleus basalis neurons could contribute to an axonal disconnection in chronic traumatic encephalopathy. PMID: 27834536
  76. Regions other than the constitutive promoter may be involved in microtubule-associated protein tau gene regulation in tauopathies. PMID: 27709663
  77. LRRK2 regulates intracellular Tau levels, contributing to the progression of the pathology caused by the LRRK2-mediated proteasome impairment. PMID: 26014385
  78. This study demonstrated that transient hypoxia may acutely increase the levels of Abeta42 and T-tau in plasma of healthy adults. PMID: 27389622
  79. findings suggest that elevated plasma t-tau levels reflect AD pathology and therefore have potential as an objective biomarker to detect dementia in adult DS PMID: 29190730
  80. Insulin is accumulated and retained as oligomers in hyperphosphorylated tau-bearing neurons in Alzheimer's disease and in several of the most prevalent human tauopathies. PMID: 29053786
  81. Inhibition of CaN attenuated the hTau-induced CREB dephosphorylation with improved synapse and memory functions. PMID: 27298345
  82. Study describes a protocol to extract and measure tau seeding activity from small volumes (.04 mm(3)) of formaldehyde-fixed tissue immediately adjacent to that used for immunohistochemistry, validated this method with the PS19 transgenic mouse model, and easily observed seeding well before the development of phospho-tau pathology. Also accurately isolated two tau strains, DS9 and DS10, from fixed brain tissues in mice. PMID: 28587664
  83. evidence that JNK signaling pathway is an upstream regulator of hyperosmotic stress-induced Tau cleavage and apoptosis in SH-SY5Y through the control of caspase-3 activation. PMID: 29126968
  84. cryo-electron microscopy (cryo-EM) maps at 3.4-3.5 A resolution and corresponding atomic models of paired helical and straight tau filaments from the brain of an individual with Alzheimer's disease PMID: 28678775
  85. Central nervous system (CNS)-derived tau in L1CAM-containing exosomes was characterized extensively in human plasma, including by single molecule array technology with 303 subjects. In human plasma, tau was explicitly identified within L1CAM exosomes. In contrast to Alzheimer's patients, L1CAM exosomal tau was significantly higher in Parkinson's patients than controls and correlated with cerebrospinal fluid tau. PMID: 27234211
  86. The authors identify conditions, where the microtubule-binding repeats of Tau undergo a phosphorylation-dependent liquid-liquid phase separation, leading to molecular crowding in the formed Tau liquid droplets and characterize them by NMR and other biophysical methods. PMID: 28819146
  87. Our findings unmask tau-mediated perturbations of specific pathways associated with neuronal vulnerability, revealing potential early disease biomarkers and therapeutic targets for FTD and other tauopathies. PMID: 27594585
  88. Our studies also provide mechanistic insight into the increased level and activity of secreted MMP-9 in cortical neurons derived from FTD patient-specific iPSCs with MAPT mutations. The increase seems to be mediated by ERK-pathway activation. PMID: 27594586
  89. The authors found that TRIM28 regulates alpha-Synuclein and tau nuclear levels and that its reduction rescues toxicity in animal models of tau- and alpha-Synuclein-mediated degeneration. PMID: 27779468
  90. atomic force microscopy reveal that full length human tau, when assembled into dense surface-bound layers, can participate in attractive electrostatic interactions consistent with the previously reported dimerization model. However, modulating the ionic strength of the surrounding solution can change the structure of these layers to produce purely repulsive interactions consistent with a polyelectrolyte brush structure. PMID: 29039655
  91. In the Brazilian population studied, the frequency of GRN mutations was 9.6% and that of MAPT mutations was 7.1%. Among familial cases of FTD, the frequency of GRN mutations was 31.5% and that of MAPT mutations was 10.5%. PMID: 27082848
  92. Association of human and mouse P-tau with amyloid PrPSc did not diminish survival time following prion infection in these mice. By analogy, human P-tau may not affect prion disease progression in humans. PMID: 27463540
  93. Besides being associated with tau pathology, CSF YKL-40 adds to the growing array of biomarkers reflecting distinct molecular brain mechanisms potentially useful for stratifying individuals for biomarker-guided, targeted anti-inflammatory therapies emerging from precision medicine. PMID: 28281838
  94. Study shows that the microtubule-associated protein tau H1 haplotype was associated with Parkinson's disease susceptibility. PMID: 27061069
  95. This study demonstrated that no significant group differences in the total group or the MAPT group at follow-up. PMID: 27625986
  96. findings are in agreement with the pathology literature, which suggests that tau tangles but not amyloid-beta plaques correlate with cognition and clinical symptoms of early Alzheimers disease patients PMID: 28334939
  97. Investigated the role of membrane surface charge on the binding affinity of individual tau repeat segments, and whether these segments exhibit lytic activity. While neutral membranes exhibited weak interactions with each tau repeat segment, segments R2 and R3 exhibited relatively strong binding with anionic membranes with favorable entropy and a negative value of specific heat capacity. PMID: 28986260
  98. Amyloidogenesis process of Tau protein has been summarized. (Review) PMID: 28833749
  99. Findings implicate a toxic axis of phosphorylation events beginning with Thr175 phosphorylation, dependent on further phosphorylation at Thr231, which appears to be neuron specific and which may be common to the tauopathies. PMID: 28077166
  100. Results demonstrate a strong association between progranulin deficiency and reduction of Tau protein expression that could lead to severe neuronal and glial dysfunctions; also indicate that this frontotemporal lobar degeneration (FTLD)-TDP-GRN subgroup could be part as a distinct entity of FTLD classification. PMID: 27435172

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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
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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