NMDA (phospho Tyr1336) Antibody | 50-233

NMDA (phospho Tyr1336) Antibody | 50-233 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Rat

Homology: N/A

Immunogen: Phosphopeptide corresponding to amino acid residues surrounding the phospho-Tyr1336 of the NR2B subunit of the rat NMDA receptor.

Research Area: Phospho-Specific, Neuroscience

Tested Application: WB, IHC

Application: The antibody has been directly tested for reactivity in Western blots with rat tissue. It is anticipated that the antibody will react with human, mouse and non-human primate tissues based on the fact that these species have 100% homology with the amino acid sequence used as antigen.

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 180

Validation: N/A

Isoform: N/A

Purification: Affinity Purified

Clonality: Polyclonal

Clone: N/A

Isotype: N/A

Conjugate: Unconjugated

Physical State: Liquid

Buffer: N/A

Concentration: N/A

Storage Condition: NMDA antibody can be stored at -20˚C and is stable at -20˚C for at least 1 year.

Alternate Name: N/A

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002) . The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993) . Phosphorylation of Tyr1336 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002) and ischemia may also increase the phosphorylation of this site (Takagi et al., 2003) .