protein

Lon Protease Protein, E. coli (His)

HY-P74772

50 μg

560 USD

Lon Protease Protein, E. coli (His)

proteins

E. coli

50 μg

560 USD

Lon protease is an ATP-dependent serine protease that selectively degrades mutant proteins, short-lived regulators, and specific antitoxins and is critical for cellular homeostasis. It is essential for survival during DNA damage and stress-induced changes by gradually degrading polypeptides into 5-10 amino acid fragments. Lon Protease Protein, E. coli (His) is the recombinant E. coli-derived Lon Protease protein, expressed by E. coli , with C-His labeled tag. The total length of Lon Protease Protein, E. coli (His) is 784 a.a., with molecular weight of ~88 kDa.

E.coli

Lon Protease, an ATP-dependent serine protease, serves as a crucial mediator in the selective degradation of mutant and aberrant proteins, as well as certain short-lived regulatory proteins, including specific antitoxins. Essential for cellular homeostasis, Lon Protease plays a pivotal role in ensuring survival under conditions of DNA damage and stress-induced developmental changes. Operating processively, this protease degrades polypeptides to generate small peptide fragments typically ranging from 5 to 10 amino acids in length. Additionally, Lon Protease exhibits a DNA-binding capacity in a double-stranded, site-specific manner. Among its endogenous substrates are regulatory proteins like RcsA, SulA, SoxS, UmuD, and various type II antitoxins such as CcdA, HipB, and MazE. Notably, Lon Protease, when overproduced, selectively impedes translation through distinct pathways, including the YoeB-YefM toxin-antitoxin system.

ATP-dependent protease La; lon; capR; deg; lopA; muc

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, 10% Glycerol, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.