Mouse monoclonal antibody (clone 2H9) recognizes the phosphorylated serine 422 of Tau proteins and is suitable for Western Blot, for Immunohistochemistry and Immunofluorescence.

The phosphorylation of Tau protein at serine 422 is a pathological epitope and a marker of neurofibrillary degeneration, one of the neuropathological hallmark of Alzheimer’s disease.

On cerebral tissue sections, Anti-Tau pS422 clone 2H9 antibody (4BDX-1501) detects specifically neurons engaged in neurofibrillary degeneration.

According to the literature, the serine 422 is phosphorylated by the following kinases: CaMKII (Calcium Calmodulin-kinase II), PKA (protein kinase A), JNKs (c-Jun N-terminal kinases), ERK1/2 or p42/44 MAKP (mitogen-activated kinases), p38 MAPK and MARK (Microtubule-associated protein/microtubule affinity-regulating kinase).

The monoclonal antibody Clone 2H9 (4BDX-1501) is directed against phospho-Ser422 and does not cross-react with the unphosphorylated Ser422 peptide. This antibody is useful by immunoblotting to detect pS422 epitope in brain homogenates from patients presenting a Tauopathy.

By immunohistochemistry, this reference has been shown to label neurofibrillary tangles in Alzheimer patients and Tau transgenic brain sections. This monoclonal antibody is also suitable for immunotherapy in experimental models of Tauopathies (Troquier et al. 2012).

This Pathological epitope at phosphorylated serine 422 of Tau is then found in Alzheimer ‘s disease, argyrophilic grain dementia (Tolnay et al., 2002) but also several other tauopathies including down syndrome, corticobasal degeneration, progressive supranuclear palsy, pick’s disease and frontotemporal dementia linked to mutation of MAPT gene (Bussière et al., 1999 ; Sergeant et al. 1999).

Phospho-serine 422 epitope as revealed by 4BDX-1501 is also observed in tau aggregates in inclusion body myotisis (Maurage et al., 2004).

Recently, the phosphorylation of tau at serine 422 was shown to protect tau from caspase cleavage (Sandhu et al., 2017).

In Alzheimer’s disease, phosphorylated tau at serine 422 is found in pre-tangle neurons (Guillozet-Bongaarts et al., 2016), and appearance of phosphorylated serine 422 tau epitope is correlate of the disease neuropathology and cognitive decline (Vana et al., 2011).

Mouse monoclonal antibody (clone 2H9) recognizes the phosphorylated serine 422 of Tau proteins and is suitable for Western Blot, for Immunohistochemistry and Immunofluorescence.

The phosphorylation of Tau protein at serine 422 is a pathological epitope and a marker of neurofibrillary degeneration, one of the neuropathological hallmark of Alzheimer’s disease.

On cerebral tissue sections, Anti-Tau pS422 clone 2H9 antibody (4BDX-1501) detects specifically neurons engaged in neurofibrillary degeneration.

According to the literature, the serine 422 is phosphorylated by the following kinases: CaMKII (Calcium Calmodulin-kinase II), PKA (protein kinase A), JNKs (c-Jun N-terminal kinases), ERK1/2 or p42/44 MAKP (mitogen-activated kinases), p38 MAPK and MARK (Microtubule-associated protein/microtubule affinity-regulating kinase).

The monoclonal antibody Clone 2H9 (4BDX-1501) is directed against phospho-Ser422 and does not cross-react with the unphosphorylated Ser422 peptide. This antibody is useful by immunoblotting to detect pS422 epitope in brain homogenates from patients presenting a Tauopathy.

By immunohistochemistry, this reference has been shown to label neurofibrillary tangles in Alzheimer patients and Tau transgenic brain sections. This monoclonal antibody is also suitable for immunotherapy in experimental models of Tauopathies (Troquier et al. 2012).

This Pathological epitope at phosphorylated serine 422 of Tau is then found in Alzheimer ‘s disease, argyrophilic grain dementia (Tolnay et al., 2002) but also several other tauopathies including down syndrome, corticobasal degeneration, progressive supranuclear palsy, pick’s disease and frontotemporal dementia linked to mutation of MAPT gene (Bussière et al., 1999 ; Sergeant et al. 1999).

Phospho-serine 422 epitope as revealed by 4BDX-1501 is also observed in tau aggregates in inclusion body myotisis (Maurage et al., 2004).

Recently, the phosphorylation of tau at serine 422 was shown to protect tau from caspase cleavage (Sandhu et al., 2017).

In Alzheimer’s disease, phosphorylated tau at serine 422 is found in pre-tangle neurons (Guillozet-Bongaarts et al., 2016), and appearance of phosphorylated serine 422 tau epitope is correlate of the disease neuropathology and cognitive decline (Vana et al., 2011).