Anti-phospho-Tau (pSer199/202) antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

MDL number:
Pricing and availability is not currently available.

biological source


Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies




buffered aqueous glycerol solution

species reactivity

mouse, rat, human


microarray: suitable
western blot: suitable



UniProt accession no.

shipped in

wet ice

storage temp.


Gene Information

human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)

General description

Tau proteins are known as microtubule-associated phosphoprotein (MAP) and express mainly in neurons of central nervous system. It has a crucial role in tubulin polymerization and facilitates microtubules assembly and stability. The biological activity of tau proteins depends on degree of its phosphorylation. Anti-phospho-Tau (pSer199/202) antibody can be used in microarray and western blotting. It can also be used in immunoblotting. Rabbit anti- phospho-Tau (pSer199/202) antibody reacts specifically with human Tau (pSer199/202) (45-68 kD).
Tau (τ), also known as MAPT (microtubule associated protein tau), is encoded by the gene mapped to human chromosome 17q21.3. It is highly expressed in neurons, but is most prominent in axons.


chemically synthesized phosphopeptide derived from the region of human tau that contains serine199 and serine202.


Anti-phospho-Tau (pSer199/202) antibody (diluted 1:1000 in PBS containing 0.3% Triton X-100 and 0.5% BSA) can be used in immunocytochemistry for identification of protein aggregates. It can also be used as primary antibody (diluted 1: 3000) in immunohistochemistry.
Anti-phospho-Tau (pSer199/202) antibody produced in rabbit has been used in:
  • immunocytochemistry
  • immunohistochemistry
  • western blot

Biochem/physiol Actions

Tau (τ) plays an essential role in the assembly and maintenance of microtubule structure. Deletion of tau (τ) results in developmental delay and learning disability. The gene expression is associated with the development of Alzheimer′s disease (AD). Genetic variation in τ gene increases the risk of susceptibility to the sporadic tauopathies, progressive supranuclear palsy (PSP) and corticobasal degeneration.

Physical form

Solution in 100 μl Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, 50% glycerol, containing 1.0 mg/ml BSA (IgG, protease free) and 0.05% sodium azide. The amount of antibody is sufficient for 10 immunoblots.


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.


Exclamation mark

Signal Word


Hazard Statements

Precautionary Statements


NONH for all modes of transport

WGK Germany


Flash Point(F)

320.0 °F - closed cup

Flash Point(C)

160 °C - closed cup

Rodrigo S Chaves et al.
BMC neuroscience, 11, 144-144 (2010-11-12)
Protein aggregates containing alpha-synuclein, beta-amyloid and hyperphosphorylated tau are commonly found during neurodegenerative processes which is often accompanied by the impairment of mitochondrial complex I respiratory chain and dysfunction of cellular systems of protein degradation. In view of this, we...
Feng-Qin Zhou et al.
Alzheimer's research & therapy, 10(1), 40-40 (2018-04-25)
Alzheimer's disease (AD) is a devastating neurodegenerative disorder bearing multiple pathological hallmarks suggestive of complex cellular/molecular interplay during pathogenesis. Transgenic mice and nonhuman primates are used as disease models for mechanistic and translational research into AD; the extent to which...
Tian Tu et al.
Frontiers in aging neuroscience, 12, 93-93 (2020-06-02)
Amyloid plaques and neurofibrillary tangles (NFTs) are hallmark lesions of Alzheimer's disease (AD) related to β-amyloid (Aβ) deposition and intraneuronal phosphorylated tau (pTau) accumulation. Sortilin C-terminal fragments (shortened as "sorfra") can deposit as senile plaque-like lesions within AD brains. The...
Eun-Bum Kang et al.
Journal of exercise nutrition & biochemistry, 19(3), 199-209 (2015-11-04)
Neurofibrillary tangles, one of pathological features of Alzheimer's disease, are produced by the hyperphosphorylation and aggregation of tau protein. This study aimed to investigate the effects of treadmill exercise on PI3K/AKT/mTOR signal transmission, autophagy, and cognitive ability that are involved...

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.