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
Beilstein:
3697262
EC Number:
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
Product Name
S-(2-Aminoethyl)-L-cysteine hydrochloride, ≥98% (TLC)
Quality Level
Assay
≥98% (TLC)
form
powder
color
white to off-white
storage temp.
2-8°C
SMILES string
Cl.NCCSC[C@H](N)C(O)=O
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
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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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Do Youn Jun et al.
Biochemical pharmacology, 66(12), 2291-2300 (2003-11-26)
We first report the mechanism for the inhibitory effect of the lysine analog, thialysine on human acute leukemia Jurkat T cells. When Jurkat T cells were treated with thialysine (0.32-2.5 mM), apoptotic cell death along with several biochemical events such
Ulf Göransson et al.
Analytical biochemistry, 318(1), 107-117 (2003-06-05)
The expression of cyclotides-macrocyclic plant peptides-was profiled in six violets, Viola cotyledon, V. biflora, V. arvensis, V. tricolor, V. riviniana, and V. odorata, by LC-MS. All were found to express notably complex mixtures, with single species containing >50 cyclotides. To
Dasantila Golemi-Kotra et al.
The Journal of biological chemistry, 279(33), 34665-34673 (2004-05-21)
Beta-lactamases and penicillin-binding proteins are bacterial enzymes involved in antibiotic resistance to beta-lactam antibiotics and biosynthetic assembly of cell wall, respectively. Members of these large families of enzymes all experience acylation by their respective substrates at an active site serine
M N Cahyanto et al.
Journal of applied microbiology, 102(3), 674-679 (2007-02-21)
To enhance L-lysine secretion in Lactobacillus plantarum. An S-2-aminoethyl-L-cystein (AEC)-resistant mutant of L. plantarum was isolated, and it produced L-lysine at considerably higher level than the parent strain. Aspartokinase in the mutant has been desensitized to feedback inhibition by L-lysine.
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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