Tyrosinase Antibody [P8H17] | Primary Antibodies

Application: Reactivity: Mouse, Human

Lane 1: Mewo

Usage Information

Dilution
WB1:1000-1:5000 IHC1:100-1:500

Application
WB, IHC

Reactivity
Mouse, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
60 kDa 50-80 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Tyrosinase Antibody [P8H17] detects endogenous levels of total Tyrosinase protein.

Clone
P8H17

Synonym(s)
Tyrosinase; LB24-AB; Monophenol monooxygenase; SK29-AB; Tumor rejection antigen AB; TYR

Background
Tyrosinase, the rate-limiting copper-containing monooxygenase of the tyrosinase family alongside TRP1 and TRP2, catalyzes the initial steps of melanogenesis by hydroxylating L-tyrosine to L-DOPA and oxidizing L-DOPA to dopaquinone through a type-3 dicopper active site featuring oxy-tyrosinase (Cu2O2) and met-tyrosinase (Cu2(OH)) intermediates. Binuclear copper coordination at His residues enables electrophilic aromatic attack, where dioxygen activation produces the μ-η2:η2-peroxo dicopper core that delivers the hydroxyl equivalent to the ortho position of monophenols, followed by two-electron oxidation of diphenols via substrate-assisted proton transfer; conformational shifts between syn/anti ligand geometries gate substrate access while latent zymogen activation by proteolysis exposes the catalytic cleft. The enzyme integrates within melanosomal complexes where TRP2 (DCT) accelerates dopachrome tautomerization, and TRP1 isomerizes quinone methides to 5,6-dihydroxyindoles, with MITF-driven transcriptional synergy at E-box/CATGTG motifs amplifying expression under UV/cAMP/PKA signaling. Tyrosinase governs constitutive and UV-inducible pigmentation in melanocytes, protecting basal keratinocytes from ROS while establishing retinal pigment epithelium barrier function critical for photoreceptor outer segment phagocytosis. OCA1A mutations abolish copper loading/trafficking, causing complete albinism with foveal hypoplasia, while hypomorphic OCA1B variants retain partial activity; conversely, melanoma exploits PKC-β phosphorylation and TPC2-mediated melanosome pH for hyperactivation, driving aberrant pigmentation that aids immunoevasion through melanin-mediated ROS quenching.

Background

Tyrosinase, the rate-limiting copper-containing monooxygenase of the tyrosinase family alongside TRP1 and TRP2, catalyzes the initial steps of melanogenesis by hydroxylating L-tyrosine to L-DOPA and oxidizing L-DOPA to dopaquinone through a type-3 dicopper active site featuring oxy-tyrosinase (Cu2O2) and met-tyrosinase (Cu2(OH)) intermediates. Binuclear copper coordination at His residues enables electrophilic aromatic attack, where dioxygen activation produces the μ-η2:η2-peroxo dicopper core that delivers the hydroxyl equivalent to the ortho position of monophenols, followed by two-electron oxidation of diphenols via substrate-assisted proton transfer; conformational shifts between syn/anti ligand geometries gate substrate access while latent zymogen activation by proteolysis exposes the catalytic cleft. The enzyme integrates within melanosomal complexes where TRP2 (DCT) accelerates dopachrome tautomerization, and TRP1 isomerizes quinone methides to 5,6-dihydroxyindoles, with MITF-driven transcriptional synergy at E-box/CATGTG motifs amplifying expression under UV/cAMP/PKA signaling. Tyrosinase governs constitutive and UV-inducible pigmentation in melanocytes, protecting basal keratinocytes from ROS while establishing retinal pigment epithelium barrier function critical for photoreceptor outer segment phagocytosis. OCA1A mutations abolish copper loading/trafficking, causing complete albinism with foveal hypoplasia, while hypomorphic OCA1B variants retain partial activity; conversely, melanoma exploits PKC-β phosphorylation and TPC2-mediated melanosome pH for hyperactivation, driving aberrant pigmentation that aids immunoevasion through melanin-mediated ROS quenching.

References
https://pubmed.ncbi.nlm.nih.gov/30596633/ https://pubmed.ncbi.nlm.nih.gov/7969144/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%