RNASEK Protein, Human (Cell-Free, His)

RNASEK proteins cleave ApU and ApG phosphodiester bonds and hydrolyze UpU bonds at a slower rate. RNASEK Protein, Human (Cell-Free, His) is the recombinant human-derived RNASEK protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of RNASEK Protein, Human (Cell-Free, His) is 137 a.a., with molecular weight of 21.5 kDa.

RNASEK Protein functions as an endoribonuclease with a preference for cleaving ApU and ApG phosphodiester bonds, demonstrating a lower rate of hydrolysis for UpU bonds. Beyond its ribonuclease activity, RNASEK plays a crucial regulatory role in the activity of vacuolar (H+)-ATPase (V-ATPase), responsible for maintaining intracellular compartment pH. Moreover, RNASEK is essential at an early stage of receptor-mediated endocytosis, influencing the intricate processes involved in cellular uptake. In the context of microbial infection, RNASEK emerges as a critical player in the early stages of both clathrin-mediated and clathrin-independent endocytic uptake of various viruses, encompassing notable pathogens such as dengue, West Nile, Sindbis, Rift Valley Fever, influenza, and human rhinoviruses. The diverse functionality of RNASEK highlights its significant contributions to cellular processes, ranging from RNA cleavage to the regulation of endocytosis, and positions it as a key factor in the cellular response to viral infections.

Human

E. coli Cell-free

N-10*His

Q6P5S7 (M1-R137)

440400

MGWLRPGPRPLCPPARASWAFSHRFPSPLAPRRSPTPFFMASLLCCGPKLAACGIVLSAWGVIMLIMLGIFFNVHSAVLIEDVPFTEKDFENGPQNIYNLYEQVSYNCFIAAGLYLLLGGFSFCQVRLNKRKEYMVR

21.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.