Phospho Ser416 Tau Antibody
Affinity purified rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
---|---|
Primary Accession | P19332 |
Reactivity | Rat |
Predicted | Bovine, Human, Mouse, Monkey |
Host | Rabbit |
Clonality | polyclonal |
Calculated MW | 59/65/68 KDa |
Gene ID | 69329 |
---|---|
Gene Name | MAPT |
Other Names | Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, Mapt, Mtapt, Tau |
Target/Specificity | Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser416 conjugated to KLH. |
Dilution | WB~~ 1:1000 |
Format | Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephospho-peptide affinity columns. |
Antibody Specificity | Specific for ~59, 65, 68k tau protein phosphorylated at Ser416. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Phospho Ser416 Tau Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
Tau is a key microtubule-associated protein that plays an important role in the formation of microtubules in axons (Binder et al. 1985). Six tau isoforms have been identified as products of a single gene produced by alternative mRNA splicing (Goedert 1990). Tau mutations have been implicated in many neurodegenerative disorders such as Alzheimer’s disease (AD), Pick’s disease and progressive supranuclear palsy. It has been well documented that hyperphosphorylated tau is a major component of paired helical filaments in AD brain (Lee 1995). Serine 416 has been demonstrated to be a major phosphorylation site in vitro by CaM kinase II (Steiner at al. 1990).
References
Binder LI, Frankfurter A, Rebhun LI (1985) The distribution of tau in the mammalian central
nervous system. J Cell Bio Oct; 101(4):1371-8.
Lee V.M.Y. (1995) Disruption of the cytoskeleton in Alzheimer’s disease. Curr. Opin. Neurobiol.
5, 663-668.
Goedert M. and Jakes R. (1990) Expression of separate isoforms of human tau protein:
correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 9, 4225-
4230.
Steiner B., Mandelkow E.M., Biernat J. et al. (1990) Phosphorylation of microtubuleassociated
protein tau: identification of the site for Ca2+-calmodulin dependent kinase and
relationship with tau phosphorylation in Alzheimer tangles. EMBO J. 9, 3539-3544.
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