ADTRP Protein, Human (Cell-Free, His, Myc)

ADTRP protein exhibits specialized enzymatic activity, specifically hydrolyzing bioactive fatty-acid esters of hydroxy-fatty acids (FAHFAs), with a notable preference for branched FAHFAs. This unique function distinguishes ADTRP, as it does not hydrolyze other major lipid classes. Moreover, ADTRP regulates endothelial cells, influencing TFPI expression and cell-associated anticoagulant activity, observed in in vitro settings. ADTRP Protein, Human (Cell-Free, His, Myc) is the recombinant human-derived ADTRP protein, expressed by E. coli Cell-free , with N-10*His, C-Myc labeled tag. The total length of ADTRP Protein, Human (Cell-Free, His, Myc) is 230 a.a., with molecular weight of 31.8 kDa.

ADTRP protein demonstrates a specialized enzymatic function, specifically hydrolyzing bioactive fatty-acid esters of hydroxy-fatty acids (FAHFAs), with a notable preference for FAHFAs exhibiting branching distal from the carboxylate head group. This distinctive enzymatic activity sets ADTRP apart, as it does not hydrolyze other major classes of lipids. Additionally, ADTRP plays a regulatory role in endothelial cells by influencing the expression and cell-associated anticoagulant activity of the inhibitor TFPI, as observed in in vitro settings.

Human

E. coli Cell-free

N-10*His;C-Myc

Q96IZ2 (M1-K230)

84830

MTKTSTCIYHFLVLSWYTFLNYYISQEGKDEVKPKILANGARWKYMTLLNLLLQTIFYGVTCLDDVLKRTKGGKDIKFLTAFRDLLFTTLAFPVSTFVFLAFWILFLYNRDLIYPKVLDTVIPVWLNHAMHTFIFPITLAEVVLRPHSYPSKKTGLTLLAAASIAYISRILWLYFETGTWVYPVFAKLSLLGLAAFFSLSYVFIASIYLLGEKLNHWKWGDMRQPRKKRK

31.8 kDa

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

<1 EU/μg, determined by LAL method.