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MAK005

Sigma-Aldrich

Phenylalanine Assay Kit

sufficient for 100 fluorometric tests

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About This Item

UNSPSC Code:
12161503
NACRES:
NA.84

usage

sufficient for 100 fluorometric tests

detection method

fluorometric

relevant disease(s)

neonatal diseases; neurological disorders; pediatric diseases

storage temp.

−20°C

General description

Phenylalanine is a non-polar essential amino acid.[1][2] In the liver, phenylalanine is converted to tyrosine, which is a precursor for multiple compounds including L-DOPA[3] and melanin. Defects in the activity of phenylalanine hydroxylase result in the inherited metabolic disorder phenylketonuria (PKU). PKU results in the build up of phenylalanine and phenylalanine metabolites, and can result in growth defects and mental retardation if not treated.[4]

Suitability

Suitable for L-phenylalanine detection in cell and tissue culture supernatants, serum, and other biological samples

Principle

Phenylalanine concentration is determined by a coupled enzyme assay, which results in the deamination of phenylalanine and the production of NADH which reacts with the probe resulting in a fluorescent (λex = 535 nm/λem = 587 nm) product, proportional to the phenylalanine present.

replaced by

Product No.
Description
Pricing

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

flash_point_f

No data available

flash_point_c

No data available

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Certificates of Analysis (COA)

Lot/Batch Number
8E23K05720
8H30K05720
7M10K05720
7J21K05720
7E24K05720

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AMINO ACIDS | Metabolism
Encyclopedia of Food Sciences and Nutrition (Second Edition) (2003)
Nathan Crook et al.
ACS synthetic biology, 9(5), 1010-1021 (2020-04-24)
The development of robust engineered probiotic therapies demands accurate knowledge of genetic construct expression in the gut. However, the monetary and ethical costs of testing engineered strains in vertebrate hosts are incompatible with current high-throughput design-build-test cycles. To enable parallel
Phenylketonuria: an inborn error of phenylalanine metabolism.
Williams R A, et al.
The Clinical Biochemist. Reviews / Australian Association of Clinical Biochemists, 29(1), 31-31 (2008)
Protein and Amino Acid Metabolism
Essentials of Medical Biochemistry null
Nathan Crook et al.
Cell host & microbe, 25(4), 499-512 (2019-03-31)
Probiotics are living microorganisms that are increasingly used as gastrointestinal therapeutics by virtue of their innate or engineered genetic function. Unlike abiotic therapeutics, probiotics can replicate in their intended site, subjecting their genomes and therapeutic properties to natural selection. We exposed
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Protocols

Enzymatic Method for Determining Phenylalanine (Phenylalanine Assay)

Assay protocol for the fluorometric detection of Phenylalanine in biological samples using the phenylalanine assay kit.

Questions

1–2 of 2 Questions  

  1. What enzymes are included in the enzyme mix for this kit? Alternatively, please specify which enzymes are not part of the enzyme mix in the kit.

    1 answer

    1. The enzyme included in the kit is capable of reacting with tyrosine, methionine, and phenylalanine. According to a specific article, L-phenylalanine dehydrogenase can convert tyrosine and methionine in addition to phenylalanine.

      It's important to note that the enzyme is isolated from bacteria, not humans. The reaction pathway, likely catalyzed by phenylalanine dehydrogenase, is as follows: L-phenylalanine + H2O + NAD+ ⇌ phenylpyruvate + NH3 + NADH + H+.

      It was mentioned that any additional information about the enzyme would be proprietary. However, it was disclosed that this proprietary enzyme aids in the conversion of phenylalanine to generate NADH. In this process, PHE is reductively deaminated with the simultaneous formation of NADH, which reacts with our fluorescent probe to produce fluorescence at Ex/Em = 535/587 nm. It is advisable to proceed with the understanding that the reaction follows the pathway outlined in my previous note.

      Helpful?

  2. What is the procedure for removing the precipitate in the assay buffer?

    1 answer

    1. To dissolve the precipitate in the assay buffer, gently heat it with swirling. Placing it in a hot water bath at 50 - 60 degrees for 10-15 minutes should suffice. Avoid vigorously shaking the assay buffer to prevent foam formation. Allow it to cool to room temperature before proceeding with the assay.

      Helpful?

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