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L-Lysine monohydrate

BioReagent, suitable for cell culture, from non-animal source

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L-Lysine hydrate (1:1), Lysine monohydrate
Empirical Formula (Hill Notation):
C6H14N2O2 · H2O
CAS Number:
Molecular Weight:
Beilstein/REAXYS Number:
EC Number:
MDL number:
PubChem Substance ID:

biological source

non-animal source

Quality Level

product line



98.5-101.5% dry basis


crystalline powder


cell culture | mammalian: suitable


endotoxin, tested




215 °C


H2O: soluble

SMILES string




InChI key


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General description

L-Lysine is an amino acid with a basic side chain and is amphipathic in nature. It has a protonated alkyl amino group and is fully protonated at physiological pH. L-lysine mainly participates in electrostatic interactions in proteins.


L-Lysine monohydrate has been used in:
  • SILAC (stable isotope labeling by amino acids in cell culture) method
  • the complete synthetic (C) medium for positive selection screening of yeast cells
  • the growth medium for cells

Biochem/physiol Actions

L-Lysine is an essential proteinogenic α amino acid used in a wide range of applications including as a non-animal sourced supplement in cell culture media, a substrate of enzymes such as L-lysine oxidase (EC, a component of poly-lysine polymers, and a substrate for oxidation and glycation mechanism studies.

Storage Class

11 - Combustible Solids




Not applicable


Not applicable


Eyeshields, Gloves, type N95 (US)

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Garrett RH and Grisham CM
Biochemistry (2016)
W L McKeehan et al.
Proceedings of the National Academy of Sciences of the United States of America, 73(6), 2023-2027 (1976-06-01)
The trace element selenium is essential for clonal growth of diploid fibroblasts from human fetal lung (WI-38) in media containing small amounts of serum protein. Maximum growth stimulation is obtained when 30 nM neutralized selenious acid is added to a
Shao-En Ong et al.
Nature protocols, 1(6), 2650-2660 (2007-04-05)
Stable isotope labeling by amino acids in cell culture (SILAC) is a simple, robust, yet powerful approach in mass spectrometry (MS)-based quantitative proteomics. SILAC labels cellular proteomes through normal metabolic processes, incorporating non-radioactive, stable isotope-containing amino acids in newly synthesized
Daniel Kalb et al.
Chembiochem : a European journal of chemical biology, 16(10), 1426-1430 (2015-05-13)
L-α-Aminoadipic acid reductases catalyze the ATP- and NADPH-dependent reduction of L-α-aminoadipic acid to the corresponding 6-semialdehyde during fungal L-lysine biosynthesis. These reductases resemble peptide synthetases with regard to their multidomain composition but feature a unique domain of elusive function--now referred
H Kusakabe et al.
The Journal of biological chemistry, 255(3), 976-981 (1980-02-10)
L-Lysine alpha-oxidase from Trichoderma viride Y244-2 has been purified to homogeneity. The enzyme shows absorption maxima at 277, 388, and 466 nm and a shoulder around 490 nm and contains 2 mol of FAD/mol of enzyme. The enzyme has a

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