추천 제품
Quality Level
분석
97%
형태
powder
광학 활성
[α]20/D +23°, c = 2 in 1 M NaOH
반응 적합성
reaction type: solution phase peptide synthesis
색상
white to off-white
mp
214 °C (dec.) (lit.)
응용 분야
detection
peptide synthesis
SMILES string
N[C@@H](CSCc1ccccc1)C(O)=O
InChI
1S/C10H13NO2S/c11-9(10(12)13)7-14-6-8-4-2-1-3-5-8/h1-5,9H,6-7,11H2,(H,12,13)/t9-/m0/s1
InChI key
GHBAYRBVXCRIHT-VIFPVBQESA-N
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Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
이미 열람한 고객
Michelle Rudden et al.
Scientific reports, 10(1), 12500-12500 (2020-07-29)
Body odour is a characteristic trait of Homo sapiens, however its role in human behaviour and evolution is poorly understood. Remarkably, body odour is linked to the presence of a few species of commensal microbes. Herein we discover a bacterial
S Mukherjee et al.
Nuclear medicine and biology, 20(4), 413-426 (1993-05-01)
To explore the possibility of utilizing cysteine derivatives for technetium-99m radiopharmaceutical preparation with clinical potential, we synthesized two benzyl substituted cysteine compounds, namely, S-benzyl cysteine 1 and cysteine benzyl ester 3. It was expected, from our previous studies on benzoyl
M Rooseboom et al.
Chemical research in toxicology, 14(1), 127-134 (2001-02-15)
Previously, it was shown that beta-elimination of selenocysteine Se-conjugates by rat renal cytosol leading to pyruvate formation was not solely catalyzed by pyridoxal phosphate-dependent enzymes. It was hypothesized that selenoxidation of the selenocysteine Se-conjugates, followed by syn-elimination, may be an
P J Sausen et al.
The Journal of biological chemistry, 265(11), 6139-6145 (1990-04-15)
Cysteine conjugate S-oxidase activity, with S-benzyl-L-cysteine as substrate, was found mostly in the microsomal fractions of rat liver and kidney. In the presence of oxygen and NADPH, S-benzyl-L-cysteine is converted to S-benzyl-L-cysteine sulfoxide; no S-benzyl-L-cysteine sulfone was detected. The Vmax
R S Phillips et al.
The Journal of biological chemistry, 266(28), 18642-18648 (1991-10-05)
Lysine 269 in Escherichia coli tryptophan indole-lyase (tryptophanase) has been changed to arginine by site-directed mutagenesis. The resultant K269R mutant enzyme exhibits kcat values about 10% those of the wild-type enzyme with S-(o-nitrophenyl)-L-cysteine, L-tryptophan, and S-benzyl-L-cysteine, while kcat/Km values are
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