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L-Carnitine inner salt has been used as a component of an assay medium for Seahorse XF mitochondrial stress assay. t has also been orally administered to tumor-bearing mice, in order to study its effect on the regulation of peroxisome proliferator-activated receptor and thereby to analyse liver inflammatory response.

Carnitine biosynthesized from lysine. Carnitine facilitates fatty acid transport into the mitochondrial compartment. In skeletal and cardiac muscle tissue it acts as a metabolic cofactor. Carnitine might be associated with the energy production from branched chain amino acids.

Carnitine is a quaternary amine that occurs naturally in most mammalian tissue. It is present in relatively high concentrations in skeletal muscle and heart where it is involved in regulating energy metabolism. It shifts glucose metabolism from glycolysis to glycogen storage and enhances the transport of long chain fatty acids into the mitochondria where they are oxidized for energy production.

L-lysine contains basic side chain and is hydrophilic in nature. The N-butyl amino group in the side chain is found to be protonated at physiological pH. Upon degradation, L-lysine gives ketone bodies. Transamination of lysine with α-ketoglutarate produces acetoacetyl CoA. L-lysine serves as a precursor for secondary metabolites, such as β-lactam antibiotics. It also serves as a precursor for the biosynthesis of α-aminoadipic acid.

L-Lysine is an essential proteinogenic α amino acid used in a wide range of applications. It has been used:
• as a supplement in cell culture media
• as a substrate for enzymes such as L-lysine oxidase (EC 1.4.3.14)
• as a component of poly-lysine polymers
• as a substrate for oxidation and glycation mechanism studies
• in the preparation of cobaltous lysine

DL-Methionine is an essential amino acid containing sulphur. Methionine consists of an asymmetric carbon and exists as D (dextrogyre) and L (levogyre) optical isomers. The L-methionine is considered as biologically active. The racemic mixture of D and L-isomers forms DL-methionine, which is the commercially available methionine.

DL-Methionine has been used to study its effect on the growth and feed utilization of Nile tilapia. It has also been used as a part of standard diet in animal models.

DL-Methionine is an amino acid that has a role in the defence of oxidative stress.

Methionine offers protection against disorders related to hair, skin and nails. It elevates lecithin production in the liver and thereby reduces cholesterol level. It naturally serves as a heavy metal chelating agent, regulating ammonia concentration in the urine. This ameliorates bladder irritation. Methionine is also known to induce hair growth.

L-arginine has been used to study non-enzymatic gluconeogenesis. It has also been used to study the effects of L-arginine supplementation on kidney and liver injury in rats with myocardial infarction.

L-Arginine is a dibasic, semi-essential amino acid. It acts as a precursor for creatinine and is a natural constituent of most of the dietary proteins.

Substrate of nitric oxide synthase, which is converted to citrulline and nitric oxide (NO). Induces insulin release by a nitric oxide-dependent mechanism.

L-Citrulline has been used in ultra-performance liquid chromatography to validate, metabolites involved in the coordination of metamorphic processes.

Intermediate in the production of nitric oxide from L-arginine by NO synthetase.

L-Citrulline, when orally administered is found to ameliorate the condition of sickle cell disease in humans. L-citrulline can be a replacement for L-arginine administration in case of defective NO synthetase. L-Citrulline supplementation is found to fulfill the purpose of NO-dependent signaling.

L-cysteine is a sulfur-containing non-essential amino acid. Its ability to reduce colitis symptoms is being assessed for potential use in treating inflammatory bowel disease (IBD).

Naturally occurring non-essential amino acid.

L-cysteine can be used as a cysteine source to prepare L-cysteine functionalized gold nanoparticles for use as probes in the colorimetric detection of Hg²⁺ in aqueous solution.

L-Cystine has been used in in vitro cystine solubility assay to identify potential drugs that influence cystine solubility. It is also used as a supplement of phosphate-buffered saline to slice and wash periprosthetic tissues.

Cysteine is the source of disulfide linkages in proteins and has a role in sulfur transport. It undergoes rapid oxidation to form cystine at physiological pH. L-cystine is crucial for oxygen production and low density lipoprotein modification by arterial smooth muscle cells. It also has a role in the synthesis of glutathione.

L-Glutamic acid has been used to enhance endogenous acetylcholine overflow. It has been used as a supplement in the growth medium of meat-Spoiling Pseudomonas fragi 72.

An excitatory amino acid neurotransmitter that is an agonist at all subtypes of glutamate receptors (metabotropic, kainate, NMDA, and AMPA).

Glutamic acid, or glutamate, the salt form of glutamic acid, functions as a neurotransmitter and also serves as a precursor to other neurotransmitters such as γ-aminobutyric acid.Glutamic acid also plays a key role in many metabolic pathways, that controls growth, reproduction, maintenance and immunity. It is converted to α-ketoglutarate, a key component of the TCA (tricarboxylic acid) cycle, and a precursor for the biosynthesis of nucleic acids and certain amino acids. In cells, glutamine is converted to glutamate by the enzyme glutaminase.
Glutamine serves as a source of energy for rapidly dividing cells comprising lymphocytes, enterocytes, macrophages and tumors. Glutamine mediates protein turnover via cellular mTOR (mammalian target of rapamycin) signaling. It is also known to be associated with the inhibition of apoptosis.

An excitatory amino acid neurotransmitter that is an agonist at all subtypes of glutamate receptors (metabotropic, kainate, NMDA, and AMPA).

Glycine is a non-chiral amino acid. Glycine is a molecule with pI of 6.7, which is similar to the pH of stacking region in polyacrylamide gels. It has advantage of low mobility, hydrophobicity and it does not associate with proteins.

• Glycine has been added in the transfer buffer during western blotting procedure.^[4]
• It has been used in the solution prepared for dissolving formazan crystals in the MTT (3-[4,5-dimethylthiazol-2-yl]-2,5 diphenyltetrazolium bromide) cytotoxicity assay.^[5]
• It has been used for terminating the rat basophilic leukemia (RBL) assay.

Glycine is an inhibitory neurotransmitter in the central nervous system and works as an allosteric regulator of NMDA (N-methyl-D-aspartate) receptors. It is involved in processing of motor and sensory data, thereby regulating movement, vision and audition.

Inhibitory neurotransmitter in spinal cord, allosteric regulator of NMDA receptors.

L-Leucine has been used as an agonist of mechanistic target of rapamycin (mTOR) to determine whether AMPK/mTOR pathway is involved in berberine-mediated autophagy in J774A.1 cells. It has also been used for the selection of transformed cells.

Leucine is a non-glucogenic, essential amino acid. It is a branched-chain amino acid that is a structural component of proteins. Leucine positively influences insulin release to eliminate toxic sugars out of the blood. The degradation of leucine leads to the formation of ketone bodies.

L-Methionine has been used in chloramine assay and malonaldehyde assay. It has also been used as a standard in methionine assay.

L-Methionine serves as precursor for transmethylation and transsulphuration. Methionine adenosylation results in the formation of S-adenosyl-L-methionine (SAM). SAM serves as a methyl donor to a number of substances. This methylation is significantly associated with the immune system functioning. Thus, SAM deficiency causes severe combined immunodeficiencies. L-Methionine’s metabolic product, glutathione, is known to regulate immune response and has antiviral action.

Phenylalanine is an amino acid. It participates in the preparation of ternary piroxicam complexes of Fe(II), Fe(III), Co(II), Ni(II), Cu(II) and Zn(II). Characterization of these complexes by elemental analyses, molar conductance, IR, UV-Vis, magnetic moment, diffuse reflectance and X-ray powder diffraction methods has been conducted. Crystalline DL-phenylalanine was prepared by its reduction in silica gel by solubility method.

DL-Phenylalanine may be used in the synthesis of ternary piroxicam (Pir; 4-hydroxy-2-methyl-N-(2-pyridyl)-2H-1,2-benzothiazine-3-carboxamide 1,1-dioxide) complexes of Fe(II), Fe(III), Co(II), Ni(II), Cu(II) and Zn(II).

L-Phenylalanine has been used in Fluo-4 Ca²⁺-assay in a study to demonstrate that G-protein coupled receptor 139 reference surrogate agonists 1a and 7c and L-phenylalanine share a common binding site.It has also been used to spike blood samples to study the effect of dried blood spots on newborn screening.

L-Phenylalanine is an essential aromatic amino acid. It has a role in metabolism as it forms a starting point for many pathways.This neutral amino acid is a precursor for tyrosine, epinephrine, dopamine and norepinephrine.

L-Proline has been used:
• As a supplement during the preparation of chondrogenic medium and synthetic dextrose minimal medium (SD).
• As a standard during the identification of metabolites in serum samples.
• In a study to prepare L-proline-L-phenylalanine (L-Pro-L-Phe) mixture in aqueous acetonitrile.

L-tryptophan has been used for the isolation of bone marrow–derived neutrophils. It has also been used to identify the use of Raman microscopy as a tool to study the network of neurons in pathologically normal retina.

Tryptophan (Trp) is a heterocyclic, essential amino acid associated with growth, reproduction and immunity. Increased availability of tryptophan is necessary for the regulation of mood, cognition and behavior. The uptake of tryptophan by the brain depends on the plasma ratio of Trp to all of the other large neutral amino acids. Higher the ratio, greater is the Trp uptake

L-Tyrosine has been used to prepare tyrosine solution for tyrosinase assay. It has also been used to assay pepsin activity.

L-Tyrosine is a non-essential amino acid with a polar side chain. It is utilized by cells to synthesize proteins that have a role in signal transduction. L-Tyrosine is a proteogenic amino acid that acts as a receiver of phosphate groups that are transferred by kinases.

• L-Valine has been used as a standard in thin layer chromatography.
• It has been used as a supplement in Grace’s antheraea medium for the culture of cells and tissue from invertebrates.
• It has been used in the preparation of starvation media to study the role of relA gene in antibiotic resistance in E. coli.

Valine is an essential amino acid, involved in the biosynthesis of glutamine and alanine. Valine being a branched-chain amino acid (BCAA) maintains a balance among the BCAAs. L-Valine serves as an energy fuel. Long term deficiency of L-Valine leads to growth failure, organ damage and loss of muscle mass.

β-Alanine has been used as a ligand for the orphan MAS-related receptor. It has also been used in culture media used for certain strains of yeast to test for β-alanine auxotrophy.

β-Alanine, a β−amino acid, is a component of pantothenic acid and the rate-limiting amino acid in the biosynthesis of the histidinyl antioxidant dipeptides carnosine and anserine. Endogenous β-amino acid that is a nonselective agonist at glycine receptors and a ligand for the G protein-coupled orphan receptor, TGR7 (MrgD). β-Alanine flux plays a cytoprotective role by supporting the osmotic stability of marine organisms, preimplantation mouse embryos and mammalian cells exposed to hypoxic stress.

Asparagine biosynthesis is catalyzed by glutamine-dependent asparagine synthetase in mammalian tissues.Elevated levels of free asparagine is observed in plants facing stress in the form of drought or high salt. It is also present in senescing leaves and germinating seeds.

L-Asparagine monohydrate has been used:
• as a component of Sauton’s and chelated Sauton’s media for mycobacterial growth
• to test its effect in the induction of Ca²⁺ flux in rice roots using aequorin luminescence imaging
• as a component of fermentation medium for the Blakeslea trispora spores

Asparagine has high nitrogen to carbon ratio and is a key regulator for nitrogen storage and transport. Its thermal degradation in the presence of sugars leads to the acrylamide formation in foods. Asparagine serves as an amino acid exchange factor and is essential for amino acid homeostasis. It favors cancer cell proliferation.

L-Asparagine, a proteinogenic amino acid, is used in biomanufacturing cell culture systems for the production of therapeutic recombinant proteins and monoclonal antibodies and in cell culture based research.

L-Isoleucine has been used in capillary feeder (CAFE) assay in a study to determine the consumption of amino acids by Drosophila melanogaster. It has also been used as one of the components of an amino acid mixture, which is used as a supplement for synthetic complete (SC) media.

L-Isoleucine is an isomer of L-leucine and is an essential amino acid. It is synthesized from threonine and is a branched-chain hydrophobic amino acid

Norvaline (abbreviated as Nva) is an amino acid with the formula CH₃(CH₂)₂CH(NH₂)CO₂H. The compound is an isomer of the more common amino acid valine. Like most other α-amino acids, norvaline is chiral. It is a white, water-soluble solid.

Norvaline is a non-proteinogenic unbranched-chain amino acid. It has previously been reported to be a natural component of an antifungal peptide of Bacillus subtilis. Norvaline and other modified unbranched chain amino acids have received attention because they appear to be incorporated in some recombinant proteins found in E. coli. Its biosynthesis has been examined. The incorporation of Nva into peptides reflects the imperfect selectivity of the associated aminoacyl-tRNA synthetase. In Miller–Urey experiments probing prebiotic synthesis of amino acids, norvaline, but also norleucine, are produced.

Norvaline is known to promote tissue regeneration and muscle growth, and to become a precursor in the penicillin biosynthetic pathway.

Norvaline has not been reported to be toxic at doses up to 5 grams a day, and it is commonly used by bodybuilders to increase muscle mass. At higher concentration, over 5 grams a day, norvaline was shown to decrease cell viability (cell concentration 125???um) and caused necrotic cell death and significant changes to mitochondrial morphology and function. At high concentrations, all amino acids are cytotoxic, and norvaline toxicity could be attributed to protein amino acid mimicry. However, the conclusions of this study have been recently questioned, because the demonstrated l-norvaline toxicity is limited to specific in vitro assays at exceedingly high concentrations. Moreover, in higher organisms, l-norvaline is well tolerated, and in vivo toxicity is not apparent.

Norvaline and norleucine (one hydrocarbon group longer) both possess the nor- prefix for historical reason, despite current conventional usage of the prefix to denote a missing hydrocarbon group (under which they would theoretically be called "dihomoalanine" and "trihomoalanine"). The name is not systematic, and the IUPAC/IUB Joint Commission on Nomenclature recommends that this name should be abandoned and the systematic name should be used.

Norvaline is a promising candidate drug for the treatment of Alzheimer's disease. It is a non-competitive arginase inhibitor which readily crosses the blood-brain barrier, and reduces arginine loss in the brain. Amyloid-beta deposition is associated with L-arginine deprivation and neurodegeneration. Mice treated with Norvaline display improved spatial memory, increased neuroplasticity-related proteins, and decrease in amyloid-beta.

L-Theanine is an analog of glutamine and a component of green tea.

L-Theanine modulates the activity of several antitumor drugs and has been reported to stimulate self-renewal of human embryonic stem cells. L-Theanine binds to AMPA, Kainate, NMDA, and group I mGlu receptors.

Theanine is able to bind to AMPA, kainite, and NMDA glycine receptors in rat cortical neurons but with less affinity than glutamic acid.  It has been studied as a glutamate transport inhibitor, preventing glutamate uptake by M5076 ovarian sarcoma-bearing mouse cells and increasing the effect of doxorubicin on tumor growth in M5076 mice. 

Theanine is an amino acid analog of glutamine, found in green tea.

DL-Alanine, a racemic mixture of D- and L-alanine, is used as a model reagent for development of amino acid racemic resolution techniques. DL-Alanine is used in mixed ligand (chelate) studies with transition metals such as Cu(II), Zn(ll) and Cd(ll).

L-Alanine, a non-essential amino acid, is produced enzymatically from L-aspartate using aspartate β-decarboxylase. It is the smallest among all the aminoacids.

L-Alanine has been used as a supplement in complete medium for cell culture.

DL-Aspartic acid (DL-Asp) is a racemic mixture of the proteinogenic amino acid L-aspartate and the non-proteinogenic amino acid D-aspartate. DL-Aspartic acid is used in studies on factors and conditions that enhance semen and sperm quality.

L-aspartic acid has been used as one of the components of synthetic drop out media for culturing budding yeast. It has also been used to study non-enzymatic gluconeogenesis.

Aspartic acid is a non-essential amino acid. It is involved in the Urea cycle, Krebs cycle and in DNA metabolism.

Principal neurotransmitter for fast synaptic excitation.

Principal neurotransmitter for fast synaptic excitation.

L-Carnosine has been used to study its effects as an antioxidant on meat quality of pigs.It has also been used to study its effects on brain injury in a rat intracerebral hemorrhage model.

L-Carosine is a dipeptide found at millimolar concentration in brain, muscle and the lens of the eye. In model systems it is a potent antioxidant that scavenges oxygen free radicals and transition metal ions. It blocks protein-protein and protein-DNA cross-links induced by hypochlorite anions and toxic aldehydes such as acetaldehyde, formaldehyde, and malondialdehyde, the primary product of lipid peroxidation. It also inhibits nonenzymatic protein glycation induced by aldose and ketose reducing sugars and inhibits the formation of toxic advanced glycation end products (AGE). These activities make it of interest in studies of aging, atherosclerosis, Alzheimer′s disease, and the secondary effects of diabetes.

Dipeptide with potent antioxidant and antiglycation activity; blocks nonenzymatic glycosylation and protein cross-linking induced by reactive aldehydes.

L-Glutamine has been used to study the effects of amino acids in promoting food consumption in Drosophila melanogaster. It has also been used to study non-enzymatic gluconeogenesis.

L-glutamine is the most abundant amino acid in the body. It is essential for the synthesis of L-asparagine. L-glutamic acid aids the incorporation of NH4⁺ into biomolecules.

L-Glutamine is an essential amino acid that is a crucial component of culture media that serves as a major energy source for cells in culture. L-Glutamine is very stable as a dry powder and as a frozen solution. In liquid media or stock solutions, however, L-glutamine degrades relatively rapidly. Optimal cell performance usually requires supplementation of the media with L-glutamine prior to use.

L-histidine has been used for the selection of transformed cells. It has also been used to study its effects on the formation of verteporfin cross-linked oligomers in cellular homogenates.

L-Histidine is an essential amino acid. It binds to metal ions and may aid in the transport of copper.  Histidine is widely present at the active sites of enzymes. It also has a role in binding of heme groups, macromolecules and phosphate groups in the binding sites of proteins.

Precursor of histamine by action of histidine decarboxylase.

Versatile reagent for the synthesis of neuroexcitatory kainoids and antifungal echinocandins. Also employed in the synthesis of chiral ligands for enantioselective ethylation of aldehydes.

Natural constituent of animal structural proteins such as collagen and elastin.

L-Pyroglutamic acid is used in the synthesis of:
• Nonproteinogenic amino acids such as (3S,4R)-3,4-dimethyl-L-pyroglutamic acid and (3S,4R)-3,4-dimethyl-L-glutamine.
• Chiral N-heterocyclic carbenes (NHCs) as catalysts for the asymmetric dimerization of alkylarylketenes to give the corresponding α-quaternary β-alkylidenyl-β-lactones.

It is also used in the total synthesis of (−)-stemoamide and celogentin C.

L-Serine has been used in the preparation of Tris-BSAN buffer for homogenization. It has also been used for quantitative analysis of excretion of polypeptides in normal urine.

L-Serine is a non-essential amino acid that acts as a precursor for nucleotide synthesis. It has roles in the development and function of the central nervous system. L-Serine also has a role in cellular proliferation.

Precursor of glycine by serine hydroxymethyltransferase.

L-threonine has been used for the selection of transformed cells. It has also been used to study the effects of amino acids in promoting food consumption in Drosophila melanogaster.

L-Threonine is an essential amino acid. It is involved in the synthesis of mucin, a protein supporting intestinal function and integrity. L-threonine has a role in the immune system, in O-linked glycosylation, protein phosphorylation and glycine synthesis.

Taurine (2-aminoethanesulphonic acid) is predominantly found in the retina and heart and is also found in the brain, intestine, skeletal muscles and kidneys.

Taurine has been used for the isolation and growth of taurine-utilizing purple non-sulfur bacteria and in phototrophic growth experiments.