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About This Item
Empirical Formula (Hill Notation):
C7H9NO2S
CAS Number:
Molecular Weight:
171.22
EC Number:
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
Recommended Products
technique(s)
ligand binding assay: suitable
SMILES string
N[C@H](Cc1cccs1)C(O)=O
InChI
1S/C7H9NO2S/c8-6(7(9)10)4-5-2-1-3-11-5/h1-3,6H,4,8H2,(H,9,10)/t6-/m1/s1
InChI key
WTOFYLAWDLQMBZ-ZCFIWIBFSA-N
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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R A Wapnir et al.
The Biochemical journal, 177(1), 347-352 (1979-01-01)
The inhibitory properties of beta-2-thienyl-dl-alanine on rat phenylalanine hydroxylase from crude liver and kidney homogenates were assessed in vitro and in vivo, as well as its effects on the intestinal transport of phenylalanine, by using a perfusion procedure in vivo.
X Liu et al.
Biopolymers, 33(8), 1237-1247 (1993-08-01)
Bradykinin (BK) is a peptide hormone with sequence Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9 and has been implicated in a multitude of pathophysiological processes such as the ability to lower systemic blood pressure and stimulate pain. BK analogues having bulky, beta-branched D-aliphatic residues at position
J J Slon-Usakiewicz et al.
Biochemistry, 39(9), 2384-2391 (2000-03-01)
Synthetic bivalent thrombin inhibitors comprise an active site blocking segment, a fibrinogen recognition exosite blocking segment, and a linker connecting these segments. Possible nonpolar interactions of the P1' and P3' residues of the linker with thrombin S1' and S3' subsites
D P Bedard et al.
Journal of bacteriology, 141(1), 100-105 (1980-01-01)
When treated with the amino acid analog beta-2-DL-thienylalanine, cells of the yeast Saccharomyces cerevisiae accumulated in the G1 portion of the cell cycle at the "start" event. This G1 arrest was accompanied by a rapid decrease in the rate of
"Physiological phenylketonuria": a biochemical defect caused by delayed maturation of the phenylalanine hydroxylation pathway and by competition with the phenylalanine biosynthetic pathway.
K J Brown
Medical hypotheses, 6(2), 215-224 (1980-02-01)
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