A2636
S-(2-Aminoethyl)-L-cysteine hydrochloride
≥98% (TLC)
Synonym(s):
L-4-Thialysine hydrochloride
Sign In to View Organizational & Contract Pricing.
Select a Size
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
Looking for similar products? Visit Product Comparison Guide
Related Categories
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)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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.
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
Divergence in noncognate amino acid recognition between class I and class II lysyl-tRNA synthetases.
Jeffrey Levengood et al.
The Journal of biological chemistry, 279(17), 17707-17714 (2004-01-30)
Lysine insertion during coded protein synthesis requires lysyl-tRNA(Lys), which is synthesized by lysyl-tRNA synthetase (LysRS). Two unrelated forms of LysRS are known: LysRS2, which is found in eukaryotes, most bacteria, and a few archaea, and LysRS1, which is found in
Brian C Jester et al.
Proceedings of the National Academy of Sciences of the United States of America, 100(24), 14351-14356 (2003-11-19)
Insertion of lysine during protein synthesis depends on the enzyme lysyl-tRNA synthetase (LysRS), which exists in two unrelated forms, LysRS1 and LysRS2. LysRS1 has been found in most archaea and some bacteria, and LysRS2 has been found in eukarya, most
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service