Key features and details
- Assay type: Quantitative
- Detection method: Colorimetric
- Platform: Microplate reader
- Sample type: Other biological fluids, Plasma, Serum, Urine
- Sensitivity: 50 µM
Product nameTyrosine Assay Kit (Colorimetric)
Sample typeUrine, Serum, Plasma, Other biological fluids
Sensitivity< 50 µM
Species reactivityReacts with: Mammals, Other species
Abcam's Tyrosine Assay Kit (Colorimetric) (ab185435) is a simple, yet sensitive assay that is able to detect normal and abnormal concentrations of Tyrosine in biological fluids. The assay is based on the enzymatic oxidation of Tyrosine producing a stable signal (OD 492 nm), which is directly proportional to the amount of Tyrosine. Sample preparation is minimal and does not require strenuous or complicated procedures. The assay can detect as low as 50 µM of Tyrosine in a variety of biological samples.
Tyrosine (Tyr) is one of the four standard amino acids containing an aromatic group as a side chain. Its hydrophobicity is one of the main characteristics of this uncharged polar amino acid. In addition to being an essential amino acid Tyr is important in number of biological processes such as the synthesis of neurotransmitters, thyroid hormones, melanine, fumarate and acetoacetate. The pathology of abnormal concentrations of Tyr is well known in diseases including phenylketonuria, hypothyroidism, tyrosinemia, albinism, and alkaptonuria.
Abcam has not and does not intend to apply for the REACH Authorisation of customers’ uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Storage instructionsStore at -20°C. Please refer to protocols.
Components 100 tests Tyr Assay Buffer 1 x 25ml Tyr Enzyme Mix 1 vial Tyr Standard 1 vial
RelevanceTyrosine (4-hydroxyphenylalanine, or 2-amino-3(4-hydroxyphenyl)-propanoic acid) is one of the 20 amino acids that are used by cells to synthesize proteins. Tyrosine cannot be completely synthesized by animals, although it can be made by hydroxylation of phenylalanine if the latter is in abundant supply. There are three structural isomers of Tyr, namely para-Tyr (p-Tyr), meta-Tyr (m-Tyr) and ortho-Tyr (o-Tyr). Enzymatically, only the first isomer (p-Tyr) is produced from L-Phe by the Phe-hydroxylase enzyme. The other two isoforms, m-Tyr and o-Tyr can be produced as a consequence of free radical attack on Phe in states with increased oxidative stress. Tyrosine is converted to DOPA by the enzyme, tyrosine hydroxylase. It plays a key role in signal transduction, since it can be tagged with a phosphate group (phosphorylated) by protein kinases to alter the functionality and activity of certain enzymes. (In its phosphorylated state, it is sometimes referred to as phosphotyrosine.) Tyrosine is also a precursor to the thyroid hormones thyroxine and tri-iodothyronine, the pigment melanin, and the biologically-active catecholamines dopamine, norepinephrine and epinephrine.
- 2 amino 3(4 hydroxyphenyl) propanoic acid
- 4 hydroxyphenylalanine
ab185435 has been referenced in 3 publications.
- Tyagi A et al. E3 Ubiquitin Ligase APC/CCdh1 Regulation of Phenylalanine Hydroxylase Stability and Function. Int J Mol Sci 21:N/A (2020). PubMed: 33260674
- Tayebi M et al. Novel Bacillus subtilis Spore-Displayed Tyrosinase Kit for Rapid Detection of Tyrosine in Urine: Pharmaceutical Applications for the Early Diagnosis of Kidney-Related Diseases. Adv Pharm Bull 9:331-334 (2019). PubMed: 31380262
- Xie Y et al. HPD degradation regulated by the TTC36-STK33-PELI1 signaling axis induces tyrosinemia and neurological damage. Nat Commun 10:4266 (2019). PubMed: 31537781