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- Frdbio
- WUHAN,CHINA
- FrdM1360-NAE
- 2025年11月09日
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- 保存条件：
<- 20℃
- 保质期：
>2 years
- 英文名：
Friendbio Science & Technology Co.,Ltd.
- 库存：
200
- 供应商：
福因德科技（武汉）有限公司
- 规格：
5μg
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文献和实验Using the scan‐x Web Site to Predict Protein Post‐Translational Modifications
spectrometry data is providing evidence that almost every protein in the cell undergoes some form of post?translational modification. We describe a protocol to use the scan?x Web site to view predicted acetylation sites in the human proteome and predicted
Typical modification sites: RGG box or RXR sequence motifs R-arginine, G-glycine, X-any aminoacid. Enzymes catalysing protein arginine methylation: PRMT1 from rat and the human homologue HRMT1L2, human PRMT2 (HRMT1L1), rat and human PRMT
RNAse A Treatment of Mouse Cells
of the quality of the used RNAse A. In our lab, we used RNAse A treatment of mouse cells (see comment 1 ) to demonstrate that the enrichment in HP1 (Heterochromatin Protein 1) proteins at pericentric heterochromatin depends on the presence of an RNA component
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