L-Glutamic Acid Hcl
L-Glutamine
L-Histidine
L-Histidine Hcl
L-Hydroxyproline
L-Isoleucine
L-Leucine
L-Lysine Acetate
L-Lysine Hcl
L-Methionine
L-Ornithine Hcl
L-Phenylalanine
L-Phenylglycine
L-Proline
L-Pyroglutamic Acid
L-Serine
L-Theanine
L-Threonine
L-Tryptophan
L-Tyrosine
L-Valine
L-Homoarginine Hcl
L-Citrulline
L-Homphenylalanine
L-Homoserine
L-Homocitrulline
DL-Alanine
DL-allo-Threonine
DL-Arginine HCL
DL-Aspartic Acid
DL-Carnitine HCL
DL-Cysteine
DL-Cystine
DL-Glutamic Acid
DL-Isoleucine
DL-Lysine Hcl
DL-Methionine
DL-Phenylalanine
DL-Phenylglycine
DL-Pyroglutamic Acid
DL-Serine
DL-Threonine
DL-Tryptophan
DL-Tyrosine
DL-Valine
DL-allo-Isoleucine
DL-Homocystine
DL-Homocysteine
DL-Homoserine
DL-Norvaline
D-Alanine
D-Arginine
D-Cycloserine
D-Cysteine
D-Glucosamine Hcl
D-Glutamic Acid
D-Glutamine
D-Histidine
D-Leucine
D-Methionine
D-Phenylglycine
D-Phenylalanine
D-Proline
D-Pyroglutamic Acid
D-Serine
D-Threonine
D-Tyrosine
D-Tryptophan
D-Valine
D-Asparagine
D-Aspartic Acid
D-Arginine Hcl
D-Histidine Hcl
D-Isoleucine
D-Norvaline
D-Ornitine Hcl

L-Arginine HCL

(CAS: 1119-34-2)

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Synonyms: (S)-2-amino-5-guanidinopentanoic acid hydrochloride, S(+)-2-amino-5- [(aminoiminomethyl)amino]pentanoic acid hydrochloride, 2-amino-5-guanidinovaleric acid hydrochloride

Molecular Formula: C6H14N4O2.HCl
Molecular Weight: 210.7
CAS Number: 1119-34-2
pI: 10.761
pKa: 1.82 (COOH), 8.99 (-NH2), 12.48 (guanido group)
Specific Rotation: 21.9 (12 mg/ml, dilute HCl, 21 C)

L-Arginine is one of the three amino acids with basic side chains, and is very hydrophilic in character. It contains a guanidino group in the side chain, and this moiety is protonated at physiological pH. Arginine is biosynthesized in the kidneys from citrulline, whose precursor is glutamate via the formation of ornithine.In amino acid degradation in vivo, arginine is hydrolyzed to urea and ornithine by arginase. Arginine can be metabolized to glutamate, which in turn is converted to -ketoglutarate for entry into the citric acid cycle. L-Arginine is used in cell culture as a component of MEM amino acids solution. Cells utilize L-arginine as a precursor for the production of nitric oxide (NO), which is an activator of guanylyl cyclase and leads to the production of the second messenger cGMP. The production of NO from cultured porcine aortic endothelial cells has been demonstrated. Virulence gene expression in a tRNA modificationdeficient mutant of Shigella flexneri has been modulated by the addition of
L-arginine. A study of the effects of L-arginine on cultured human osteoblasts has been reported, with relation to bone metabolism and growth. An investigation of varying the environment for growth of Escherichia coli between growth in the presence of excess nitrogen (ammonia) to nitrogen starvation, where L-arginine is used as an alternate nitrogen source, has been reported.
Preparation Instructions: This product is soluble in water (50 mg/ml), yielding a clear, colorless solution.
Storage/Stability: Solutions of L-arginine may be autoclaved. Aqueous solutions of this product are strongly alkaline and tend to absorb carbon dioxide from the atmosphere on standing.

References:
1. Molecular Biology LabFax, Brown, T. A., ed., BIOS Scientific Publishers Ltd. (Oxford, UK: 1991), p.29.
2. The Merck Index, 12th ed., Entry# 817.
3. Biochemistry, 3rd ed., Stryer, L., W. H. Freeman (New York, NY: 1988), pp. 20, 500, 501, 505.
4. Textbook of Biochemistry with Clinical Correlations, 5th ed., Devlin, T. M., ed., Wiley-Liss (New York, NY: 2002), pp. 97, 789, 791, 871.
5. Palmer, R. M., et al., Vascular endothelial cells synthesize nitric oxide from L-arginine. Nature,333(6174), 664-666 (1988).
6. Durand, J. M., and Bjork, G. R., Putrescine or a combination of methionine and arginine restores virulence gene expression in a tRNA modificationdeficient mutant of Shigella flexneri: a possible role in adaptation of virulence. Mol. Microbiol., 47(2), 519-527 (2003).
7. Torricelli, P., et al., L-arginine and L-lysine stimulation on cultured human osteoblasts.Biomed. Pharmacother., 56(10), 492-497 (2002).
8. Atkinson, M. R., et al., Activation of the glnA, glnK, and nac promoters as Escherichia coli undergoes the transition from nitrogen excess growth to nitrogen starvation. J. Bacteriol., 184(19), 5358-5363 (2002).