protein

KYNU/Kynureninase Protein, Human (sf9, His)

HY-P75903

5 μg;10 μg;20 μg;50 μg

95;155;245;470 USD

KYNU/Kynureninase Protein, Human (sf9, His)

proteins

Sf9 insect cells

5 μg;10 μg;20 μg;50 μg

95;155;245;470 USD

KYNU, a multifaceted enzyme, plays a pivotal role in the catabolism of tryptophan by catalyzing the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Demonstrating a preference for the L-3-hydroxy form, KYNU exhibits cysteine-conjugate-beta-lyase activity, showcasing its versatility in various metabolic pathways. KYNU/Kynureninase Protein, Human (sf9, His) is the recombinant human-derived KYNU/Kynureninase protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of KYNU/Kynureninase Protein, Human (sf9, His) is 465 a.a., with molecular weight of ~47 kDa.

Human

Kynureninase (KYNU) is a pivotal enzyme that catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Notably, KYNU exhibits a preference for the L-3-hydroxy form in its enzymatic activity. In addition to its role in the kynurenine pathway, KYNU displays cysteine-conjugate-beta-lyase activity, adding another layer to its functional versatility. This enzymatic versatility positions KYNU as a key player in the metabolism of tryptophan-derived compounds, highlighting its significance in regulating the levels of bioactive molecules such as anthranilic acid and 3-hydroxyanthranilic acid, and emphasizing its broader involvement in cellular processes.

Kynureninase; L-kynurenine hydrolase; KYNU; EC:3.7.1.3

Greater than 90% as determined by reducing SDS-PAGE

Supplied as a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 8.0, 25% gly.

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