PeptideDB

O-Propargyl-Puromycin

CAS: 1416561-90-4 F: C24H29N7O5 W: 495.53

O-Propargyl-Puromycin, an alkyne analog of puromycin, is a potent protein synthesis inhibitor.
Data collection:peptidedb@qq.com

This product is for research use only, not for human use. We do not sell to patients.

Bioactivity O-Propargyl-Puromycin, an alkyne analog of puromycin, is a potent protein synthesis inhibitor.
Invitro O-propargyl-puromycin can be used to image and affinity-purify nascent proteins in cells and in animals. O-propargyl-puromycin inhibits protein synthesis, both in reticulocyte lysates and in cultured cells, displaying a potency two- to threefold lower than that of unmodified puromycin. O-propargyl-puromycin forms covalent conjugates with nascent polypeptide chains, which are rapidly turned over by the proteasome and can be visualized or captured by copper(I)-catalyzed azide-alkyne cycloaddition. [1].
In Vivo Tissues from uninjected mice shows low nonspecific staining, whereas tissues from O-propargyl-puromycin-injected mice display specific patterns of O-propargyl-puromycin incorporation into nascent proteins. In the small intestine, translation is strongest in cells in the crypts and at the base of intestinal villi, consistent with the high proliferative and secretory activity of these cells. The stain is particularly strong in Paneth cells, which are located close to the base of the crypts and are filled with secretory vesicles. The intense O-propargyl-puromycin labeling of vesicles in Paneth cells suggests that prematurely terminated, O-propargyl-puromycin-conjugated secretory proteins are translocated into the endoplasmic reticulum (ER) lumen[1].
Name O-Propargyl-Puromycin
CAS 1416561-90-4
Formula C24H29N7O5
Molar Mass 495.53
Appearance Solid
Transport Room temperature in continental US; may vary elsewhere.
Storage
Powder -20°C 3 years
4°C 2 years
In solvent -80°C 6 months
-20°C 1 month
Reference [1]. Liu J, et al. Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin. Proc Natl Acad Sci U S A. 2012 Jan 10;109(2):413-8.