Anti-Puromycin Antibodies Illuminate the World of Cellular Protein Translation

The Ribopuromycylation (RPM) technology, developed by Dr. Jon Yewdell and Dr. Alexandre David, offers a powerful and universal method for visualizing and studying protein translation within cells. RPM involves the use of puromycin, a molecule that mimics a tyrosyl-tRNA and terminates translation by becoming covalently incorporated into the nascent protein chain's C-terminus within the ribosome's A site. This technique enables the immobilization of puromycylated nascent protein chains on ribosomes when chain elongation inhibitors like cycloheximide or emetine are utilized.

Recombinant Sulfated HIV Envelope Protein and Methods for Making Protein

This technology comprises sulfated recombinant gp120 proteins and peptides. Also included are methods for producing sulfated recombinant gp120 proteins. The focus of this technology is on sulfation of two tyrosines in the V2 loop of the HIV major envelope glycoprotein, gp120, which increase the stability of gp120 and promote the synthesis of gp120 protein in its native "closed" conformation. Gp120 in its native form is highly sulfated; however, recombinant gp120 produced for vaccines or structural analyses typically display low levels of V2 tyrosine sulfation.
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