ARG51842
anti-Tau phospho (Ser416) antibody
anti-Tau phospho (Ser416) antibody for Western blot and Rat
Neuroscience antibody; Signaling Transduction antibody; Neuron Development Study antibody
Overview
| Product Description | Rabbit Polyclonal antibody recognizes Tau phospho (Ser416) |
|---|---|
| Tested Reactivity | Rat |
| Tested Application | WB |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Target Name | Tau |
| Antigen Species | Rat |
| Immunogen | Peptide sequence around phosphorylation site of serine 416 (T-G-S(p)-I-D) derived from Rat Tau. |
| Conjugation | Un-conjugated |
| Alternate Names | TAU; Neurofibrillary tangle protein; Paired helical filament-tau; PPND; DDPAC; FTDP-17; MTBT2; Microtubule-associated protein tau; PHF-tau; MSTD; PPP1R103; MTBT1; MAPTL |
Application Instructions
| Application Suggestion |
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| Application Note | * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. |
Properties
| Form | Liquid |
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| Purification | Antibodies were produced by immunizing rabbits with KLH-conjugated synthetic phosphopeptide. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. In addition, non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide. |
| Buffer | PBS (without Mg2+ and Ca2+, pH 7.4), 150mM NaCl, 0.02% Sodium azide and 50% Glycerol. |
| Preservative | 0.02% Sodium azide |
| Stabilizer | 50% Glycerol |
| Concentration | 1 mg/ml |
| Storage Instruction | For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. |
| Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
| Database Links | |
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| Background | Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy-terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by ERK, GSK-3 and CDK5 (1-2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease and these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation of Ser396 by GSK-3 or CDK5 destabilizes microtubules in Alzheimer's disease. Furthermore, inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3). |
| Research Area | Neuroscience antibody; Signaling Transduction antibody; Neuron Development Study antibody |
| Calculated MW | 79 kDa |
| PTM | Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1: CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Phosphorylation decreases with age. Phosphorylation within tau/MAP's repeat domain or in flanking regions seems to reduce tau/MAP'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. Phosphorylation at Ser-548 by GSK3B reduces ability to bind and stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons. There is a reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces glycosylation by a factor of 2 and 4 respectively. Phosphorylation on Ser-721 is reduced by about 41.5% by GlcNAcylation on Ser-717. Dephosphorylated at several serine and threonine residues by the serine/threonine phosphatase PPP5C. 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. O-glycosylated. O-GlcNAcylation content is around 8.2%. There is reciprocal down-regulation of phosphorylation and O-GlcNAcylation. Phosphorylation on Ser-717 completely abolishes the O-GlcNAcylation on this site, while phosphorylation on Ser-713 and Ser-721 reduces O-GlcNAcylation by a factor of 2 and 4 respectively. O-GlcNAcylation on Ser-717 decreases the phosphorylation on Ser-721 by about 41.5%. Glycation of PHF-tau, but not normal brain TAU/MAPT. 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. |
