INTERACTORS OF MYC ASSOCIATED ZINC FINGER PROTEIN (MAZ)

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 我们从HeLa细胞中亲和纯化了MAZ，并用MALDI-MS对共刺激蛋白进行了分析，唯一鉴定的蛋白是角蛋白。实验重复进行，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。角蛋白仅存在于60 kDa的凝胶区(内源性？)。此外，1D SDS PAGE凝胶的对照车道与IP车道没有显著差异。唯一明显的区别是MAZ。这可以是降解产物，也可以是全长MAZ的替代剪接产物。我们不断优化样品的纯化条件。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 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.