INTERACTORS OF MYC ASSOCIATED ZINC FINGER PROTEIN (MAZ)

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 我们从HeLa细胞中亲和纯化了MAZ，并通过Maldi MS分析了共纯化蛋白。 重复该实验，特别注意不要用外源性角蛋白污染样品。 同样，唯一确定的蛋白质是角蛋白。 仅在~60 kDa凝胶泳道中鉴别出角蛋白（内源性？）。 此外，1D SDS PAGE凝胶的对照泳道与IP泳道无显著差异。 唯一可见的差异被确定为MAZ。 这可能是全长MAZ的降解产物或选择性剪接产物。我们继续优化样品纯化条件。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. We have affinity purified MAZ from HeLa cells and analyzed the copurifying proteins by Maldi MS. The only protein identified was keratin. The experiment was repeated paying special care not to contaminate the sample with exogenous keratin. Again, the only protein identified was keratin. Keratin was only identified in the ~60 kDa gel lane (endogenous?). In addition, the control lane of a 1D SDS page gel did not differ significantly from the IP lane. The only visible difference was identified as MAZ. This could either be a degradation product or an alternative splicing product of full length MAZ. We continue to optimize the sample purification conditions.