(r)-proline

3-Methyl-N-{[(2-methyl-2-propanyl)oxy]carbonyl}-L-valyl-(4R)-4-hydroxy-L-proline is a pharmaceutical intermediate employed in the synthesis of various active compounds.

(R)-pyrrolidine-2-carboxylic acid (D-Proline) is an isomer of the naturally occurring amino acid L-Proline. D-amino acids, including D-Proline, are found in relatively high abundance in human plasma and saliva, potentially originating from bacterial sources or endogenous production via amino acid racemase activity.

Grb2 SH2 Domain Inhibitor 1 TFA is a cyclic cell-penetrating peptide (CPP) featuring a conformationally restricted d-pro-l-pro motif ring (AF Φ Rpprrfq), where Φ represents L-naphthylalanine, R signifies D-arginine, and P stands for D-proline. It primarily functions as a cyclic peptide inhibitor.

Grb2 SH2 Domain Inhibitor 1 is a cyclic cell-penetrating peptide (CPP) featuring a conformationally restricted d-pro-l-pro motif ring (AF Φ Rpprrfq), where Φ represents L-naphthylalanine, R denotes D-arginine, and P indicates D-proline. This compound primarily functions as a cyclic peptide inhibitor.

Trypsin/Lys-C complex protease (MS grade) combines two recombinant proteases, Trypsin and Lys-C, to efficiently hydrolyze peptide bonds. Trypsin specifically cleaves at the C-terminal of arginine (R) and lysine (K), while Lys-C targets the C-terminal of lysine (K). This combination overcomes issues of missed cleavages due to Trypsin's slower digestion at lysine and arginine, PTM alterations on lysine, or hydrophobic C-termini like proline. It is suitable for digesting complex protein samples that are difficult to process enzymatically. This protease is used for protein characterization, single-cell omics, and large-cohort proteomics studies.