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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.26
storage temp.
2-8°C
Quality Level
SMILES string
Cl.NC(=N)c1ccccc1
InChI
1S/C7H8N2.ClH/c8-7(9)6-4-2-1-3-5-6;/h1-5H,(H3,8,9);1H
InChI key
LZCZIHQBSCVGRD-UHFFFAOYSA-N
Storage Class Code
10 - Combustible liquids
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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Ryan Walsh et al.
Integrative biology : quantitative biosciences from nano to macro, 3(12), 1197-1201 (2011-11-01)
Enzyme inhibitors are usually classified as competitive, non-competitive or mixed non-competitive. Each of these designations has a serious limitation in that it only describes an extreme of inhibitory behaviour. The non-competitive inhibition equation only considers an approach to complete inhibition
Ignasi Buch et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(25), 10184-10189 (2011-06-08)
The understanding of protein-ligand binding is of critical importance for biomedical research, yet the process itself has been very difficult to study because of its intrinsically dynamic character. Here, we have been able to quantitatively reconstruct the complete binding process
Dian Jiao et al.
Journal of computational chemistry, 30(11), 1701-1711 (2009-04-29)
We have calculated the binding free energies of a series of benzamidine-like inhibitors to trypsin with a polarizable force field using both explicit and implicit solvent approaches. Free energy perturbation has been performed for the ligands in bulk water and
N Balasubramanian et al.
Parasite immunology, 32(3), 165-175 (2010-04-20)
A trypsin-like serine protease was purified by gel filtration and anion-exchange chromatography from the excretory-secretory products of parasitic phase Steinernema carpocapsae. The purified protease exhibited a molecular mass of about 29 kDa by SDS-PAGE and displayed a pI of 6.3.
Nikola Loncar et al.
Archives of insect biochemistry and physiology, 74(4), 232-246 (2010-06-16)
Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had
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