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Tyrosinase (human), (recombinant) (His-tag)

BML-SE535-0100 100 µg 319.00 USD
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Product Specification

Alternative Name:Monophenol monooxygenase
MW:~52kDa (SDS-PAGE)
Source:Produced in E. coli.
UniProt ID:P14679
Formulation:Liquid. In 50mM TRIS/HCl, pH 8.0, 1M NaCl, 0.05% Empigen BB, and 30% glycerol.
Purity:≥85% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Activity:One microgram of BML-SE535 will produce greater than 90pmol of adduct at 37°C using 0.5mM L-Tyrosine as substrate in 50mM potassium phosphate, pH 7.3, 2% dimethylformamide, 5mM MBTH (3-methyl-2-benzothiazolinone hydrazone) and monitoring formation of dopachrome-MBTH adduct at 484nm (ε484=22,300 M-1cm-1). NOTE: tyrosinases, in particular mammalian tyrosinase, are inherently inefficient enzymes, with typical changes in OD only in the deciOD range, although the reaction reaches maximal velocity quickly (typically within two minutes). In addition, its substrates and MBTH are very unstable; make stocks fresh and keep sealed in the dark until use. Lifetime and rate of enzymatic activity can be increased by the addition of CuCl to the assay buffer, but this will increase background and may complicate other redox reactions in the assay.
Application Notes:Useful tool to study enzyme kinetics and screen for inhibitors.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Handling:Avoid freeze/thaw cycles.
Scientific Background:Tyrosinase is a copper-containing enzyme that catalyzes four steps in the melanin and catecholamine synthesis pathways. Like tyrosine hydroxylase (EC, it can catalyze the formation of L-DOPA in the brain and nervous system. It oxidizes monophenols, but like catecholoxidase (EC, it can also oxidize o-diphenols to o-quinones. It is involved in cancer, Parkinson’s, pigmentation diseases, Alzheimer’s and obesity. Much of the research and inhibitor screening has used mushroom tyrosinase. However, mushroom tyrosinase interacts very differently with substrates and inhibitors compared to the human enzyme. In addition, commercially available mushroom tyrosinase is not always of good purity. Recombinant versions of human tyrosinase amino acids 1-345 or 1-378, also available commercially, are not functional due the lack of critical catalytic and structural residues.
BML-SE535 AA 12071104
Tyrosinase Activity: Formation of dopachrome-MBTH adduct monitoring at 484nm in a 96-well half area microwell plate with a range of enzyme loads. Maximum signal plateau was reached rapidly at 37°C, preventing an accurate time-dependent measurement.
BML-SE535 SDS-PAGE 12071104
SDS-PAGE Analysis. Lane 1: MW Marker, Lane 2: 2 µg Tyrosinase.
BML-SE535 structure
Melanin and catecholamine synthesis pathways
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BML-SE535 AA 12071104 BML-SE535 SDS-PAGE 12071104 BML-SE535 structure

Product Literature References

Interaction of small molecules with human tyrosinase: A surface plasmon resonance and molecular docking study: S. Patil, et al.; Int. J. Biol. Macromol. 92, 1123 (2016), Application(s): Enzyme activity assay; Surface plasmon resonance (SPR) studies; Screening and kinetic analysis; In silico docking, Abstract;

General Literature References

Evidence for the ectopic synthesis of melanin in human adipose tissue: M. Randhawa, et al.; FASEB J. 23, 835 (2009), Abstract;
Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes: S.R. Setty, et al.; Nature 454, 1142 (2008), Abstract;
A. Rescigno, et al.; Enzyme Microb. Technol. 41, 620 (2007),
A review on spectrophotometric methods for measuring the monophenolase and diphenolase activities of tyrosinase: F. Garcia-Molina, et al.; J. Agric. Food Chem. 55, 9739 (2007), Abstract;
A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations: T. Schweikardt, et al.; Pigment Cell Res. 20, 394 (2007), Abstract;
Discovery of small-molecule inhibitors of tyrosinase: J.P. Germanas, et al.; Bioorg. Med. Chem. Lett. 17, 6871 (2007), Abstract;
Naturally occurring tyrosinase inhibitors: mechanism and applications in skin health, cosmetics and agriculture industries: S. Parvez, et al.; Phytother. Res. 21, 805 (2007), Abstract;
Similar enzyme activation and catalysis in hemocyanins and tyrosinases: H. Decker, et al.; Gene 398, 183 (2007), Abstract;
Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer’s disease mutation: R. Wang, et al.; PNAS 103, 353 (2006), Abstract;
S.-H. Jeon, et al.; Bull. Korean Chem. Soc. 26, 1135 (2005),
Dopamine- or L-DOPA-induced neurotoxicity: the role of dopamine quinone formation and tyrosinase in a model of Parkinson’s disease: M. Asanuma, et al.; Neurotox. Res. 5, 165 (2003), Abstract;
Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase: M. Rios, et al.; J. Neurosci. 19, 3519 (1999), Abstract;
Mutational mapping of the catalytic activities of human tyrosinase: R.K. Tripathi, et al.; J. Biol. Chem. 267, 23707 (1992), Abstract;

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