MeCP2 (Ser-80), Phosphospecific Antibody

Product Specifications

Background

Methyl-CpG Binding Protein 2 (MeCP2) was identified based on its affinity for methylated cytosines within DNA. As a chromatin-associated multifunctional protein, MeCP2 has been implicated in regulation of transcription and chromatin structure. Mutations of MeCP2 cause Rett syndrome, which results from neuronal dysfunction and impairment in cognitive and motor functions. Regulation of MeCP2 activity may involve phosphorylation at multiple sites. Ser-421 in MeCP2 is phosphorylated in response to neuronal activity, calcium influx, and is dependent on Cam-KII. Alanine mutation of Ser-421 leads to defects in synapse development and activity. Ser-80 in MeCP2 is phosphorylated in HeLa nuclear extracts and neurons. Alanine mutation of Ser-80 attenuates MeCP2 chromatin association and leads to locomotor deficits in transgenic knock-in mice. Thus, phosphorylation of MeCP2 may be important for altering its function during neuronal activity.

Synonyms

Methyl-CpG-Binding2

Swiss Prot

Q9Z2D6

Modification Site

Ser-80

Host

Rabbit

Cross Reactivity

Human, Mouse, Rat

Target

MeCP2 (Ser-80)

Clonality

Polyclonal

Isotype

IgG

Conjugation

Unconjugated

Source

Phospho-MeCP2 (Ser-80) synthetic peptide (coupled to KLH) corresponding to amino acid residues surrounding serine 80 in mouse MeCP2.

Applications

WB, IHC

Purification

Antigen Affinity purification

Dilution

WB (1:300-5000), IHC ()

Buffer

PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Modification

Phosphorylation

Storage Conditions

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Specificity

The antibody detects a 75 kDa* protein corresponding to the molecular mass of MeCP2 on SDS-PAGE immunoblots of human PC3 cells treated with calyculin A and in mouse brain tissue. These reactivities are not observed after lambda phosphatase treatment. This peptide sequence is highly conserved in rat and human MeCP2, and has low homology to other nuclear proteins.