Tryptophan Assay Kit (Fluorometric)
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(3 Publications)
Tryptophan Assay Kit (Fluorometric) (ab211098) provides a convenient method to quantify tryptophan present in serum and urine.
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Tryptophan
- FuncS
Supplier Data
Functional Studies - Tryptophan Assay Kit (Fluorometric) (AB211098)
Typical Tryptophan standard calibration curve.
- FuncS
Supplier Data
Functional Studies - Tryptophan Assay Kit (Fluorometric) (AB211098)
Estimation of Tryptophan in human urine and serum (TTRP, total, and FTRP, free). To measure TTRP and FTRP levels in serum, samples were deproteinized using the kit protocol. Serum total Tryptophan (10 μL, undiluted), serum free Tryptophan (30 μL, undiluted), and urine (25 μL, 10-fold diluted). Samples were assayed following the kit protocol. Estimated concentrations of Tryptophan : total Tryptophan in serum : 44.2 μM; free Tryptophan in serum : 13.7 μM; bound Tryptophan in serum : 30.5 μM; Total Tryptophan in urine : 32.6 μM.
Product details
Tryptophan Assay Kit (Fluorometric) (ab211098) provides a convenient method to quantify tryptophan present in serum and urine. The assay can detect bound tryptophan in urine and free and bound tryptophan in serum. The assay principle is based on a non-enzymatic reaction that uses tryptophan as a building block, producing an intermediate product that reacts with a catalyst in order to generate a fluorophore that can be detected at Ex/Em = 370/440 nm.
The reaction is specific for Tryptophan and other amino acids do not interfere with the assay. The assay can detect as little as 2.5 uM of tryptophan in a variety of biological samples.
Other Notes
This product was previously called K557 Biovision Tryptophan Assay Kit (Fluorometric). Biovision was acquired by Abcam in 2021.
Tryptophan (TRP, W) is one of the eight essential amino acids, and is mainly used for protein synthesis. Additionally, Tryptophan serves as a building block for several metabolites including kynurenine, serotonin, tryptamine, melatonin, niacin, and NAD/NAPD. Tryptophan is the only amino acid that can be found in blood in two forms: bound (BTRP) and free (FTRP) Tryptophan. Changes in tryptophan concentrations are directly related to a number of physiological and behavioral processes including: sleep, memory, depression, motion sickness, bipolar disorders, and schizophrenia. In general, tryptophan is the least abundant amino acid in humans. External sources of tryptophan include chicken, tuna, bananas, cheese, chocolate etc. Chemically, tryptophan side chain (indole) confers its unique fluorometric properties.
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Changes in NO-L-Tryptophan influence proteins involved in cellular signaling and immune responses given its role as an oxidative stress marker. Its presence can disrupt the normal function of tryptophan-incorporating proteins which may participate in different complexes. For example the disruption can affect enzyme-substrate interactions and receptor-ligand bindings impacting cellular communication and regulatory control.
Pathways
NO-L-Tryptophan impacts oxidative pathways that engage in cellular stress response. Notably it partakes in signal transduction pathways that regulate cell survival and apoptosis. Its relations extend to proteins such as nitrated tyrosines which are similarly modified amino acids involved in signaling cascades influencing inflammation pathways like the NF-kB pathway. Disruption in these interactions leads to altered inflammatory responses.
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Publications (3)
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Biology direct 19:132 PubMed39707545
2024
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Journal of Cancer 15:4417-4429 PubMed38947391
2024
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FASEB journal : official publication of the Federation of American Societies for Experimental Biology 35:e21697 PubMed34085740
2021
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