Anti-phospho-Neph1 (Tyr637/638) Antibody

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

"Mods – modifications – small alterations can have a big impact on form and function. In the motorsports world, stock vehicles are modified to enhance their performance. Modifications, or mods, to the engine, drive train, intake and exhaust components add up to provide phenomenal performance gains that can be measured as horsepower and torque increases, which yield a competitive advantage, and result in reduced run times. In biology, proteins undergo modifications that alter their function. Some proteins require the modifications in order to perform their function effectively, whether it’s a pro-protein that is cleaved to produce an active enzyme, or a protein that is phosphorylated to facilitate a signaling process. Other proteins, such as histones, undergo modifications that regulate gene expression and alter cellular function. There are several post translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination that impact protein function and activity. As a result, the analysis of proteins and their post-translational modifications are particularly important for the study of normal and disease-associated processes. New antibodies to detect phospho Histidines are now available from EMD Millipore."