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Merck

N8513

Sigma-Aldrich

L-Norleucine

suitable for amino acid analysis, BioReagent

Sinónimos:

(S)-(+)-2-Aminohexanoic acid, (S)-2-Aminocaproic acid

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About This Item

Fórmula lineal:
CH3(CH2)3CH(NH2)CO2H
Número de CAS:
Peso molecular:
131.17
Beilstein/REAXYS Number:
1721750
EC Number:
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26

product name

L-Norleucine, suitable for amino acid analysis, BioReagent

product line

BioReagent

Quality Level

form

powder or crystals

color

white

mp

>300 °C (lit.)

suitability

suitable for amino acid analysis

application(s)

detection

SMILES string

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

InChI

1S/C6H13NO2/c1-2-3-4-5(7)6(8)9/h5H,2-4,7H2,1H3,(H,8,9)/t5-/m0/s1

InChI key

LRQKBLKVPFOOQJ-YFKPBYRVSA-N

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Application

Highly purified internal standard for all amino acid analysis methods.

Other Notes

Non-essential amino acid.

pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


Certificados de análisis (COA)

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Alborz Mahdavi et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(1), 433-438 (2013-12-19)
Pathogenic microbes have evolved complex secretion systems to deliver virulence factors into host cells. Identification of these factors is critical for understanding the infection process. We report a powerful and versatile approach to the selective labeling and identification of secreted
Silvia Lisa et al.
Cellular and molecular life sciences : CMLS, 67(16), 2825-2838 (2010-05-11)
The conversion of the cellular prion protein (PrP(C)) into its disease-associated form (PrP(Sc)) involves a major conformational change and the accumulation of sulfoxidized methionines. Computational and synthetic approaches have shown that this change in the polarity of M206 and M213
Troy Cellmer et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(15), 6103-6108 (2011-03-29)
Determining the rate of forming the truly folded conformation of ultrafast folding proteins is an important issue for both experiments and simulations. The double-norleucine mutant of the 35-residue villin subdomain is the focus of recent computer simulations with atomistic molecular
Amar R Mohite et al.
The Journal of organic chemistry, 77(12), 5423-5428 (2012-05-24)
A short, concise synthesis of enantiopure, side chain-modified α-amino acids such as 4-oxo-L-norvaline, 6-oxo-L-homonorleucine, and 5-cis-alkyl prolines is described. Knoevenagel condensation of l-aminocarboxylate-derived β-ketoesters with aldehydes followed by reductive decarboxylation results in unnatural α-amino acids in good yield. A fluorescent
Haiyan Wei et al.
The journal of physical chemistry. B, 114(36), 11820-11826 (2010-08-24)
Following the studies of urea denaturation of β-hairpins using molecular dynamics, in this paper, molecular dynamics simulations of two peptides, a 35 residue three helix bundle villin headpiece protein HP-35 and its doubly norleucine-substituent mutant (Lys24Nle/Lys29Nle) HP-35 NleNle, were undertaken

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