All Photos(1)
About This Item
Empirical Formula (Hill Notation):
C13H14N2O2
CAS Number:
Molecular Weight:
230.26
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.26
assay
≥98% (TLC)
form
powder
color
off-white
storage temp.
−20°C
SMILES string
N[C@@H](CO)C(=O)Nc1ccc2ccccc2c1
InChI
1S/C13H14N2O2/c14-12(8-16)13(17)15-11-6-5-9-3-1-2-4-10(9)7-11/h1-7,12,16H,8,14H2,(H,15,17)/t12-/m0/s1
InChI key
JOPLDMLMXHNTAX-LBPRGKRZSA-N
signalword
Warning
hcodes
pcodes
Hazard Classifications
Carc. 2
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type P3 (EN 143) respirator cartridges
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 P Chapot-Chartier et al.
European journal of biochemistry, 224(2), 497-506 (1994-09-01)
Streptococcus thermophilus CNRZ 302 contains at least three general aminopeptidases able to hydrolyze Phe-beta-naphthylamide substrate. The gene encoding one of these aminopeptidases was cloned from a total DNA library of S. thermophilus CNRZ 302 constructed in Escherichia coli TG1 using
J R Klein et al.
European journal of biochemistry, 228(3), 570-578 (1995-03-15)
A genomic library of Lactobacillus delbrueckii subsp. lactis DSM7290 DNA fragments from a Sau3A partial digestion in the low-copy-number vector pLG339, was used to screen Escherichia coli for the presence of peptidases. Using the chromogenic substrate leucine-beta-naphthylamide (Leu-NH-Nap) and E.
Proteolytic cleavage of the puromycin-sensitive aminopeptidase generates a substrate binding domain.
Zhangliang Ma et al.
Archives of biochemistry and biophysics, 415(1), 80-86 (2003-06-13)
The puromycin-sensitive aminopeptidase was found to be resistant to proteolysis by trypsin, chymotrypsin, and protease V8 but was cleaved into an N-terminal 60-kDa fragment and a C-terminal 33-kDa fragment by proteinase K. The two proteinase K fragments remain associated and
Koshiro Migita et al.
Bioscience, biotechnology, and biochemistry, 70(5), 1110-1117 (2006-05-24)
To elucidate the mechanisms involved in the increase in free amino acids during postmortem storage of meat, a novel aminopeptidase was purified from bovine skeletal muscle by ammonium sulfate fractionation and successive chromatographies such as DEAE-cellulose, Sephacryl S-200, Hydroxyapatite, Phenyl-Sepharose
Active Filters
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
