MAB5430 | Anti-Tau Antibody, Caspase Cleaved (truncated at Asp421)

100 µg  
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      Replacement Information

      Key Specifications Table

      Species Reactivity Key Applications Host Format Antibody Type
      H ELISA, IHC, WB M Purified Monoclonal Antibody
      Catalogue Number MAB5430
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      Description Anti-Tau Antibody, Caspase Cleaved (truncated at Asp421)
      Product Information
      Format Purified
      Presentation Purified immunoglobulin. Liquid in PBS. Contains no preservative.
      Application Anti-Tau Antibody, Caspase Cleaved (truncated at Asp421) is an antibody against Tau for use in ELISA, WB, IH.
      Key Applications
      • ELISA
      • Immunohistochemistry
      • Western Blotting
      Application Notes Western blot



      Optimal working dilutions must be determined by end user.
      Biological Information
      Immunogen Peptide corresponding to the C-terminus of tau truncated as aspartic acid 421.
      Epitope Caspase Cleaved (truncated at Asp421)
      Clone tau-C3
      Concentration Please refer to the Certificate of Analysis for the lot-specific concentration.
      Host Mouse
      Specificity Reacts with Tau, caspase cleaved (truncated at Asp421). The antibody shows no reactivity with full length tau nor other tau C-terminal truncations. The antibody stains amyloid beta treated neurons and brain tissue in Alzheimer's disease, more specifically it stains a subset of neurofibrillary tangles, tau-containing neuritic plaques and neuropil threads.
      Isotype IgG1
      Species Reactivity
      • Human
      Antibody Type Monoclonal Antibody
      Entrez Gene Number
      Entrez Gene Summary This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
      Gene Symbol
      • MAPT
      • PPND
      • MGC138549
      • DDPAC
      • PHF-tau
      • MTBT1
      • FLJ31424
      • TAU
      • MSTD
      • FTDP-17
      • tau
      • MAPTL
      • MTBT2
      UniProt Number
      UniProt Summary FUNCTION: SwissProt: P10636 # 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.
      SIZE: 758 amino acids; 78878 Da
      SUBUNIT: Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated.
      SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.
      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.DEVELOPMENTAL STAGE: Four-repeat (type II) tau is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain.
      DOMAIN: SwissProt: P10636 The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.
      PTM: Phosphorylation at serine and threonine residues in S-P or T- P motifs by proline-directed protein kinases (PDPK: CDC2, CDK5, GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in PHF-tau), and at serine residues in K- X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) in Alzheimer diseased brains. Phosphorylation decreases with age. Phosphorylation within tau's repeat domain or in flanking regions seems to reduce tau's interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser- 622, Ser-641 and Ser-673 in several isoforms during mitosis. & Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur. & Glycation of PHF-tau, but not normal brain tau. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD.
      DISEASE: SwissProt: P10636 # In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). & Defects in MAPT are a cause of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274, 172700]; also called frontotemporal dementia (FTD) or historically termed Pick complex. This form of frontotemporal dementia is characterized by presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. & Defects in MAPT are a cause of pallido-ponto-nigral degeneration (PPND) [MIM:168610]. The clinical features include ocular motility abnormalities, dystonia and urinary incontinence, besides progressive parkinsonism and dementia. & Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease. & Defects in MAPT are a cause of progressive supranuclear palsy (PSP) [MIM:601104, 260540]; also known as Steele-Richardson- Olszewski syndrome. PSP is characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613. & Defects in MAPT may be a cause of hereditary dysphasic disinhibition dementia (HDDD) [MIM:607485]. HDDD is a frontotemporal dementia characterized by progressive cognitive deficits with memory loss and personality changes, severe dysphasic disturbances leading to mutism, and hyperphagia.
      SIMILARITY: Contains 4 Tau/MAP repeats.
      Molecular Weight 43 kDa (aa 1 to 421) or smaller fragments with Asp421 as the c-terminus
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage Conditions Maintain at 2-8°C in undiluted aliquots for up to 6 months after date of receipt.
      Packaging Information
      Material Size 100 µg
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS)  

      Certificates of Analysis

      TitleLot Number
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2115573 2115573
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2123658 2123658
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2138456 2138456
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 1987468 1987468
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2005929 2005929
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2037193 2037193
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2051382 2051382
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2055295 2055295
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2153558 2153558
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2324394 2324394
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - 2494063 2494063
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - LV1833247 LV1833247
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - NG1742781 NG1742781
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - NG1896096 NG1896096
      Anti-Tau, Caspase Cleaved (truncated at Asp421) - NG1914808 NG1914808


      Reference overviewSpeciesPub Med ID
      Apoptosis in transgenic mice expressing the P301L mutated form of human tau.
      Rita M Ramalho, Ricardo J S Viana, Rui E Castro, Clifford J Steer, Walter C Low, Cecília M P Rodrigues
      Molecular medicine (Cambridge, Mass.) 14 309-17 2008

      Show Abstract Full Text Article
      Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease.
      Guillozet-Bongaarts, Angela L, et al.
      Neurobiol. Aging, 26: 1015-22 (2005) 2005

      Show Abstract
      The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration.
      Park, So-Young and Ferreira, Adriana
      J. Neurosci., 25: 5365-75 (2005) 2005

      Show Abstract
      Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease.
      Horowitz, Peleg M, et al.
      J. Neurosci., 24: 7895-902 (2004) 2004

      Show Abstract
      Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease.
      Gamblin, T Chris, et al.
      Proc. Natl. Acad. Sci. U.S.A., 100: 10032-7 (2003) 2003

      Show Abstract

      Data Sheet

      Anti-Tau, Caspase Cleaved (truncated at Asp421) - Data Sheet

      Newsletters / Publications

      Research Focus - Volume 2, 2013

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      Life Science Research > Antibodies and Assays > Primary Antibodies