A2636
S-(2-Aminoethyl)-L-cysteine hydrochloride
≥98% (TLC)
Synonym(s):
L-4-Thialysine hydrochloride
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About This Item
Empirical Formula (Hill Notation):
C5H12N2O2S · HCl
CAS Number:
Molecular Weight:
200.69
NACRES:
NA.26
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352209
EC Number:
223-862-1
MDL number:
Beilstein/REAXYS Number:
3697262
Product Name
S-(2-Aminoethyl)-L-cysteine hydrochloride, ≥98% (TLC)
InChI
1S/C5H12N2O2S.ClH/c6-1-2-10-3-4(7)5(8)9;/h4H,1-3,6-7H2,(H,8,9);1H/t4-;/m0./s1
InChI key
CVHKULVNPGAEQM-WCCKRBBISA-N
SMILES string
Cl.NCCSC[C@H](N)C(O)=O
assay
≥98% (TLC)
form
powder
color
white to off-white
storage temp.
2-8°C
Quality Level
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Biochem/physiol Actions
S-(2-Aminoethyl)-L-cysteine (AEC) hydrochloride is used as a lysine analogue for comparative analysis with other lysine analogues. S-(2-Aminoethyl)-L-cysteine is an alternative substrate useful for characterizing lysine cyclodeaminase from Streptomyces pristinaespiralis. AEC may be used as a non-antibiotic selection agent for genetically engineered soybeans expressing a lysine insensitive DHPS gene. AEC is being studied as an amino acid antibiotic.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Yuko Kanemaru et al.
Journal of bacteriology, 195(17), 3845-3853 (2013-06-25)
Thermus thermophilus exhibits hypersensitivity to a lysine analog, (S)-2-aminoethyl-cysteine (AEC). Cosmid libraries were constructed using genomes from two AEC-resistant mutants, AT10 and AT14, and the cosmids that conferred AEC resistance on the wild-type strain were isolated. When the cosmid library
Anne Daly et al.
Nutrients, 12(8) (2020-08-23)
In Phenylketonuria (PKU), the peptide structure of the protein substitute (PS), casein glycomacropeptide (CGMP), is supplemented with amino acids (CGMP-AA). CGMP may slow the rate of amino acid (AA) absorption compared with traditional phenylalanine-free amino acids (Phe-free AA), which may
Sandro F Ataide et al.
ACS chemical biology, 2(12), 819-827 (2007-12-25)
Structural and functional diversity among the aminoacyl-tRNA synthetases prevent infiltration of the genetic code by noncognate amino acids. To explore whether these same features distinguish the synthetases as potential sources of resistance against antibiotic amino acid analogues, we investigated bacterial
Ayako Yoshida et al.
Journal of molecular biology, 368(2), 521-536 (2007-03-14)
Aspartate kinase (AK) catalyzes the first step of the biosynthesis of the aspartic acid family amino acids, and is regulated via feedback inhibition by end-products including Thr and Lys. To elucidate the mechanism of this inhibition, we determined the crystal
Weilie Zhang et al.
Biochemistry, 46(35), 10113-10121 (2007-08-10)
Penicillin-binding proteins (PBPs) and beta-lactamases are members of large families of bacterial enzymes. These enzymes undergo acylation at a serine residue with their respective substrates as the first step in their catalytic events. Penicillin-binding protein 5 (PBP 5) of Escherichia
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