TYR Protein, Human (P.pastoris, His)
Based on 3 publication(s) in Google Scholar
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.
- Species: Human
- Source: P. pastoris
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
Description
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.
Background
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.
Publications (3)
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Journal Impact Factor
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Most Recent
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Food Chem
Discovery of anti-melanogenic components in persimmon (Diospyros kaki) leaf using LC-MS/MS-MN, AlphaFold2-enabled virtual screening and biological validation. [Abstract]2024 Oct 15:455:139814. PMID: 38824735 -
J Agric Food Chem
Unraveling the Antimelanogenic Potential of Poria cocos: Component Characterization, Spatial Distribution, and Inhibitory Mechanisms. [Abstract]2026 Jun 10;74(22):17165-17184. PMID: 42220209 -
Biosensors (Basel)
2024 Apr 19;14(4):202. PMID: 38667195
Technical Parameters
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Species Human
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Source P. pastoris
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Tag N-6*His
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Accession
P14679-1 (H19-V377)
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Molecular Construction
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N-term
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6*His
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TYR (H19-V377)
Accession # P14679-1 -
C-term
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Protein Length
Partial
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Synonyms
Tyr; Tyrosinase; EC 1.14.18.1; Albino locus protein; Monophenol monooxygenase; Tumor rejection antigen AB; SK29-AB; LB24-AB
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AA Sequence
HFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQV
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Predicted Molecular Mass
42.7 kDa
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Molecular Weight
Approximately 48 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
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Glycosylation
Yes
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Purity
≥ 85%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (237 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)