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Figure 1. MeCP2 neither copurifies nor cofractionates with the SWI/SNF complex.
(a,b) Coomassie- and silver-stained SDS gels showing MeCP2 immunopurified (IP) from mouse brain using our antibody (''Hu''). Control lanes show immunoprecipitation using protein A beads alone (''No antibody''), or using antibody beads without extract (''No extract''). Asterisks indicate contaminating polypeptides. The unusual gel mobility of MeCP2 is likely to be due to its abnormal amino acid composition: 20% of the residues are positively charged. (c) Immunoblotting shows that MeCP2 immunoprecipitated from mouse brain contains no detectable SWI/SNF components (brm, BRG1, BAF 155 and BAF 170). The MeCP2 antibody in this IP was kindly provided by P. Jones4 and was used in Harikrishnan''s study. The nuclear extract (input), the supernatant after IP (SN), and the immunoprecipitated polypeptides (IP) are indicated. The Hu antibody was used in the immunoblotting analysis. (d) A silver-stained SDS gel shows proteins immunoprecipitated from HeLa nuclear extract with antibodies to MeCP2 and SWI/SNF components, including Brm (N-19), BRG1 and brm (J1), and BAF57. The two polypeptides of about 75 kDa were both identified as MeCP2 by mass spectrometry, which probably correspond to the two splicing isoforms of MeCP2. The polypeptide marked as MeCP2e1 contained the N-terminal peptide derived from the exon 1. (e) Immunoblotting shows that MeCP2 does not coimmunoprecipitate with brm and other SWI/SNF components in HeLa extracts. (f) Immunoblotting shows that MeCP2 in a HeLa nuclear extract fractionates separately from brm and other SWI/SNF components by Superose 6 gel-filtration chromatography. Fractions corresponding to marker proteins with known molecular weight are indicated at bottom.
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