Description
Key facts
Detection method:Fluorescent,
Sample types:Urine, Serum,
Assay type:Quantitative,
Sensitivity:= 2.5 µM,
Assay Platform:Microplate reader
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.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
NO-L-Tryptophan sometimes referred to as Nitrated Tryptophan is an altered form of the amino acid tryptophan. Mechanically nitration involves the addition of a nitro group (-NO2) to the tryptophan molecule affecting its structural properties. The mass of the NO-L-Tryptophan molecule increases due to nitration. This modification occurs under oxidative stress conditions when nitrogen species are prevalent. NO-L-Tryptophan does not show tissue-specific expression as it results from post-translational modifications in various cellular conditions.
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.
NO-L-Tryptophan links to conditions such as neurodegenerative diseases and cardiovascular disorders. Overproduction of nitrated proteins in diseases like Alzheimer's associates with protein misfolding and aggregation contributing to pathogenesis. Moreover its connection with inflammatory proteins may elucidate mechanisms of atherosclerosis whereby excessive nitrated modifications exacerbate vascular inflammation and plaque formation.
