The Threonine Assay Kit (ab239726) allows for highly sensitive quantification of L-Threonine levels in biological fluids and tissues.
Fluorescent
The Threonine Assay Kit (ab239726) allows for highly sensitive quantification of L-Threonine levels in biological fluids and tissues.
Fluorescent
Microplate reader
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The Threonine Assay Kit (ab239726) allows for highly sensitive quantification of L-Threonine levels in biological fluids and tissues. The assay is based on the selective, NAD+-coupled enzymatic metabolism of threonine, yielding an oxidized intermediate and NADH. A developer enzyme mixture utilizes the NADH generated to convert the probe into a stable fluorophore (Ex/Em = 535/587 nm). The assay is not affected by physiological concentrations of other amino acids, is high-throughput adaptable and can detect threonine levels down to 2 μM in samples.
Sample Type:
This product is manufactured by BioVision, an Abcam company and was previously called K463 PicoProbe™ Threonine Assay Kit (Fluorometric). K463-100 is the same size as the 100 test size of ab239726.
This supplementary information is collated from multiple sources and compiled automatically.
Threonine often abbreviated as Thr or referred to as L-Threonine is an essential amino acid with a molecular mass of about 119.12 g/mol. This amino acid is not synthesized by the human body and must be obtained through diet. Threonine is widely expressed in many tissues due to its importance as a building block of protein biosynthesis. It contributes to protein structure and function by engaging in critical hydrogen bonding facilitated by its side chain containing a hydroxyl group which supports protein folding and stability.
This amino acid plays several roles beyond protein synthesis. Threonine acts as a precursor for glycine and serine in metabolic processes and participates in the immune function by supporting the production of antibodies. Its involvement in the synthesis of mucin proteins highlights its importance in gut health. Threonine is also part of the complex that involves tissue development and acts synergistically with other proteins in maintaining the balance of neural networks.
Threonine is integral to cellular metabolism particularly within the threonine degradation pathway that leads to acetyl-CoA production. This pathways intersections with the citric acid cycle a central metabolic hub. Furthermore threonine is also connected to the mTOR signaling pathway which regulates cell growth and proliferation. Proteins like serine and methionine have a close metabolic relationship with threonine sharing metabolic intermediates and pathways.
Altered threonine metabolism can relate to immunodeficiency disorders. It influences production of immunoglobulins in the immune system. Additionally irregular threonine levels have been observed in patients with inflammatory bowel diseases such as Crohn's disease due to its role in mucin synthesis for gut lining integrity. Both conditions highlight the amino acid's interaction with proteins like mucin and various immunoglobulins important for maintaining normal physiological functions.
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Specificity for detection of L-Threonine (L-THR) over D-Threonine and other common amino acids.
At a 10-fold molar excess (5 nmole/well) versus L-Threonine (500 pmole/well), all other amino acids tested contribute ≤5% interference.
Estimation of total L-Threonine in pooled normal human plasma (10 μl), single donor off-the-clot human serum (5 μl) and pooled human CSF (10 μl).
L-Threonine concentrations for plasma, serum and CSF samples were 93.26 ± 3.72 μM, 159.7 ± 8.36 μM and 70.92 ± 3.12 μM, respectively. Data are mean ± SEM of at least 3 replicates, samples were deproteinized using 10 kDa MWCO spin columns and assayed according to the kit protocol.
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