{"product_id":"biolegend-648812","title":"Biolegend, 648812, Purified anti-Tau, 404-441 Antibody, 25μg","description":"\u003cp\u003eTau proteins are microtubule-associated proteins (MAPs) which are abundant in neurons of the central nervous system, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes and elsewhere. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is active primarily in the distal portions of axons providing microtubule stabilization as well as flexibility. Pathologies and dementias of the nervous system such as Alzheimer's disease feature tau proteins that have become defective and no longer stabilize microtubules properly. As a result, tau forms aggregates with specific structural properties referred to as Paired Helical Filaments (PHFs) that are a characteristic of many different types of dementias, known as tauopathies.  Tau has two primary ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in human brain tissue, and they are distinguished by the number of binding domains. Three isoforms have three binding domains and the remaining three have four binding domains. The binding domains are in the carboxy-terminus of the protein and are positively-charged (for binding to the negatively-charged microtubule). Tau isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains.  Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They also differ in either zero, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-binding regions at the C-terminus. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). Tau is also a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. Phosphorylation has been reported on approximately 30 of these sites in normal tau proteins. Mechanisms that drive tau lesion formation in the highly prevalent sporadic form of AD are not fully understood, but appear to involve abnormal post-translational modifications (PTMs) that influence tau function, stability, and aggregation propensity.\u003cbr\u003e\n25μg\u003cbr\u003e\nVerified Reactivity: Human\u003cbr\u003e\nAntibody Type: Monoclonal\u003cbr\u003e\nHost Species: Mouse\u003cbr\u003e\nImmunogen: Recombinant fragment of human Tau, 404-441\u003cbr\u003e\nFormulation: Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide\u003cbr\u003e\nPreparation: The antibody was purified by affinity chromatography.\u003cbr\u003e\nConcentration: 0.5 mg\/mL\u003cbr\u003e\nStorage \u0026amp; Handling: The antibody solution should be stored undiluted between 2°C and 8°C.\u003cbr\u003e\nApplication: WB - Quality tested IHC-P, ICC - Verified\u003cbr\u003e\nRecommended Usage: Each lot of this antibody is quality control tested by western blotting. For western blotting, the suggested use of this reagent is 0.25 - 1.0 µg\/mL. For immunohistochemistry, a concentration range of 1.0 - 10.0 µg\/mL is suggested. For immunocytochemistry, a concentration range of 2.5 - 10.0 μg\/mL is recommended. It is recommended that the reagent be titrated for optimal performance for each application.\u003cbr\u003e\nAdditional Product Notes: For use in immunohistochemistry on formalin-fixed paraffin-embedded tissue (IHC-P), it is recommended to perform antigen retrieval using either Citrate Buffer, 10X (Cat. No. 420902) or Tris-EDTA pH 9.0 Antigen Retrieval Buffer (10X) (Cat. No. 422704). For use in immunocytochemistry (ICC), it is recommended to fix\/permeabilize with either of the following: -Fixation buffer (Cat. No. 420801) with 0.5 % Triton X-100 -Fixation buffer (Cat. No. 420801) with 100% ice-cold methanol\u003cbr\u003e\nRRID: AB_3717182 (BioLegend Cat. No. 648812) AB_3717182 (BioLegend Cat. No. 648813)\u003cbr\u003e\nStructure: Unmodified Tau isoforms have a molecular weight ranging from 33-79 kD. Additional high and low molecular weight Tau variants have been observed in brain tissues.\u003cbr\u003e\nDistribution: Tissue distribution: Central nervous system, peripheral ganglia and nerves, kidney, skeletal, and heart muscle Cellular distribution: Cytoskeleton, nucleus, plasma membrane, and cytosol\u003cbr\u003e\nFunction: Tau promotes microtubule assembly and stability. The short tau isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.\u003cbr\u003e\nInteraction: Tau interacts with: Sequestosome-1, Peptidyl-prolyl cis-trans isomerase FKBP4, Casein kinase I isoform delta, Serine\/threonine-protein kinase Sgk1, Laforin, and alpha-synuclein.\u003cbr\u003e\nBiology Area: Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation\u003cbr\u003e\nMolecular Family: Tau\u003cbr\u003e\nAntigen References: Meredith JE Jr, et al. 2013. PLoS One. 8:e76523. Goodall CA, et al. 2006. J. Neurol. Neurosurg. Psychiatry. 77:89. Wang Y and Mandelkow E. 2016. Nat. Rev. Neurosci. 17:5-21.\u003cbr\u003e\nGene ID: 4137\u003cbr\u003e\nUniProt: View information about Tau on UniProt.org\u003cbr\u003e\nClone: A24041E\u003cbr\u003e\nRegulatory Status: RUO\u003cbr\u003e\nOther Names: Microtubule-associated protein tau, PHF-tau, paired helical filament-tau, neurofibrillary tangle, microtubule-associated protein tau, isoform 4, G protein beta1\/gamma2 subunit-interacting factor 1, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND\u003cbr\u003e\nIsotype: Mouse IgG1, κ\u003c\/p\u003e","brand":"Biolegend","offers":[{"title":"Default Title","offer_id":46866079318185,"sku":"648812","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/products\/biolegend-648812","provider":"Iright","version":"1.0","type":"link"}