protein

Lipoate-protein ligase A/LplA Protein, E.coli (His-SUMO)

HY-P71524

5 μg;10 μg;50 μg

182;309;865 USD

Lipoate-protein ligase A/LplA Protein, E.coli (His-SUMO)

proteins

E. coli

5 μg;10 μg;50 μg

182;309;865 USD

Lipoic acid protein ligase A (LplA) is a key enzyme involved in the activation and transfer of lipoic acid, an important cofactor, to the lipoyl domain of lipoic acid-dependent enzymes. LplA catalyzes the ATP-dependent activation of exogenous lipoic acid, converting it to lipoyl-AMP as an intermediate. Lipoate-protein ligase A/LplA Protein, E.coli (His-SUMO) is the recombinant E. coli-derived Lipoate-protein ligase A/LplA protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag. The total length of Lipoate-protein ligase A/LplA Protein, E.coli (His-SUMO) is 338 a.a., with molecular weight of ~53.9 kDa.

E.coli

Lipoate-protein ligase A (LplA) is a crucial enzyme involved in the activation and transfer of lipoate, a vital cofactor, onto the lipoyl domains of lipoate-dependent enzymes. LplA catalyzes the ATP-dependent activation of exogenously supplied lipoate, converting it into lipoyl-AMP, which serves as an intermediate. This activated lipoyl-AMP is then utilized by LplA to transfer the lipoyl moiety onto target proteins. By facilitating this transfer process, LplA ensures the proper functioning of lipoate-dependent enzymes, which are involved in various essential metabolic pathways such as the citric acid cycle and the metabolism of fatty acids. Understanding the mechanisms and regulation of LplA-mediated lipoate activation and transfer can provide insights into cellular energy metabolism and the maintenance of metabolic homeostasis.

lplA; BWG_4078Lipoate-protein ligase A; EC 6.3.1.20; Lipoate--protein ligase

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

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.