Human MAPT ELISA Kit

Alternative name
Human neurofibrillary tangle protein ELISA Kit;Human paired helical filament-tau ELISA Kit;Human PHF-tau ELISA Kit;Human MAPTL ELISA Kit;Human MTBT1 ELISA Kit;Human TAU ELISA Kit;Human DDPAC ELISA Kit;Human FTDP-17 ELISA Kit;Human MSTD ELISA Kit;Human MTBT2 ELISA Kit;Human PPND ELISA Kit;Human PPP1R103 ELISA Kit;Human microtubule associated protein tau ELISA Kit;Human microtubule-associated protein tau ELISA Kit;Human G protein beta1/gamma2 subunit-interacting factor 1 ELISA Kit;Human protein phosphatase 1, regulatory subunit 103 ELISA Kit;
Catalog
E024516
species
Human
GeneMAPT
Other Species Human C MAPT/C TAU ELISA Kit Human C-MAPT/C-TAU ELISA Kit Mouse C-MAPT/C-TAU ELISA Kit Mouse Mapt ELISA Kit Bovine MAPT ELISA Kit Goat MAPT ELISA Kit Rat Mapt ELISA Kit
SpecificityThis assay has high sensitivity and excellent specificity for detection of Human MAPT. No significant cross-reactivity or interference between Human MAPT and analogues was observed.
SamplesSerum, Plasma , tissue homogenates,Cell culture supernates,Other biological fluids.
Sensitivity3.9 pg/ml
Intended UseHuman MAPT ELISA Kit allows for the in vitro quantitative determination of MAPT , concentrations in serum, Plasma , tissue homogenates and Cell culture supernates and Other biological fluids.
StorageStore the whole ELISA kit at 4℃
Product Description
specificalIntroduction: Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases. Principle of the Assay: The microtiter plate provided in this kit has been pre-coated with an antibody specific to Tau. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific for Tau and Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. Then a TMB (3,3',5,5' tetramethyl-benzidine) substrate solution is added to each well. Only those wells that contain Tau, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of a sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450 nm +/- 2 nm. The concentration of Tau in the samples is then determined by comparing the O.D. of the samples to the standard curve.
Human Microtubule-associated protein tau Protein information
Uniprot ID TAU_HUMAN
Uniprot AC Q5CZI7; Q5XWF0; Q6QT54; Q9UDJ3; Q9UMH0; Q9UQ96;
UniGene Hs.101174;
GeneID 4137
KEGG hsa:4137;
Human Microtubule-associated protein tau Protein SEQUENCE
SEQUENCE 758 AA; 78928 MW; D46C66CDBCD196E8 CRC64;
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT
PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG
TTAEEAGIGD TPSLEDEAAG HVTQEPESGK VVQEGFLREP GPPGLSHQLM
SGMPGAPLLP EGPREATRQP SGTGPEDTEG GRHAPELLKH QLLGDLHQEG
PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA QDGRPPQTAA
REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE
FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD
LPEPSEKQPA AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS
AKTLKNRPCL SPKHPTPGSS DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG
SSGAKEMKLK GADGKTKIAT PRGAAPPGQK GQANATRIPA KTPPAPKTPP
SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP KKVAVVRTPP
KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD
LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG
GGQVEVKSEK LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK
AKTDHGAEIV YKSPVVSGDT SPRHLSNVSS TGSIDMVDSP QLATLADEVS
ASLAKQGL
UCSC uc002ijr.5; human. [P10636-1];

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Human MAPT ELISA Kit