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A3784

L-Arginine

suitable for cell culture, suitable for insect cell culture, ≥98% (TLC)

Synonym(s):

(S)-2-Amino-5-guanidinopentanoic acid

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About This Item

Linear Formula:
H2NC(=NH)NH(CH2)3CH(NH2)CO2H
CAS Number:
74-79-3
Molecular Weight:
174.20
EC Number:
200-811-1
UNSPSC Code:
12352209
MDL number:
MFCD00002635
Beilstein/REAXYS Number:
1725413
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assay

≥98% (TLC)

technique(s)

cell culture | insect: suitable, cell culture | mammalian: suitable

mp

222 °C (dec.) (lit.)

SMILES string

N[C@@H](CCCNC(N)=N)C(O)=O

InChI

1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/t4-/m0/s1

InChI key

ODKSFYDXXFIFQN-BYPYZUCNSA-N

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Biochem/physiol Actions

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

Storage Class

13 - Non Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
049H03895
040K0331
018H11375

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Jia-Yi Dong et al.
American heart journal, 162(6), 959-965 (2011-12-06)
Previous studies suggest that L-arginine, an amino acid and a substrate of nitric oxide synthase, may have blood pressure (BP)-lowering effect. Because some studies were performed with limited number of patients with hypertension and therefore limited statistical power with sometimes
Diane N Singhroy et al.
Retrovirology, 10, 73-73 (2013-07-23)
Protein arginine methyltransferase 6 (PRMT6) is a nuclear enzyme that methylates arginine residues on histones and transcription factors. In addition, PRMT6 inhibits HIV-1 replication in cell culture by directly methylating and interfering with the functions of several HIV-1 proteins, i.e.
Kaoru Kumazaki et al.
Nature, 509(7501), 516-520 (2014-04-18)
Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates into the membrane, thereby facilitating membrane protein assembly in bacteria; the homologous proteins Oxa1 and Alb3 have
Vivianne J Goosens et al.
Biochimica et biophysica acta, 1843(8), 1698-1706 (2013-10-22)
The twin-arginine protein translocation (Tat) system has a unique ability to translocate folded and co-factor-containing proteins across lipid bilayers. The Tat pathway is present in bacteria, archaea and in the thylakoid membranes of chloroplasts and, depending on the organism and
Thiago S Álvares et al.
Sports medicine (Auckland, N.Z.), 41(3), 233-248 (2011-03-15)
Dietary supplements containing L-arginine, a semi-essential amino acid, are one of the latest ergogenic aids intended to enhance strength, power and muscle recovery associated with both aerobic and resistance exercise. L-arginine is claimed to promote vasodilation by increasing nitric oxide
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