protein

TYR Protein, Human (P.pastoris, His)

HY-P71792

5 μg;10 μg;50 μg

158;269;753 USD

TYR Protein, Human (P.pastoris, His)

proteins

P. pastoris

5 μg;10 μg;50 μg

158;269;753 USD

TYR protein, a copper-containing oxidase, initiates melanin production by catalyzing the hydroxylation of tyrosine to DOPA. This essential step is rate-limiting in the synthesis of melanins and polyphenolic compounds. TYR further enables the oxidation of DOPA to DOPA-quinone and potentially mediates the conversion of DHI to indole-5,6 quinone, playing a crucial role in the intricate cascade of reactions involved in melanin biosynthesis. TYR Protein, Human (P.pastoris, His) is the recombinant human-derived TYR protein, expressed by P. pastoris , with N-His, N-6*His labeled tag. The total length of TYR Protein, Human (P.pastoris, His) is 359 a.a., with molecular weight of ~48 kDa.

Human

TYR protein is a copper-containing oxidase crucial for pigment formation, playing a pivotal role in the synthesis of melanins and various polyphenolic compounds. Acting as the initiator of the melanin production pathway from tyrosine, TYR catalyzes the initial and rate-limiting step, hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine). Furthermore, it facilitates the oxidation of DOPA to DOPA-quinone and potentially mediates the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone, contributing to the complex cascade of reactions involved in melanin biosynthesis.

ATN; CMM8; LB24 AB; LB24-AB; OCA1; OCA1A; OCAIA; Oculocutaneous albinism IA; SHEP3; SK29 AB; SK29-AB; Tumor rejection antigen AB; TYR; Tyrosinase

Greater than 85% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.