B6388
Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin
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关于此项目
经验公式（希尔记法）:
C33H43N7O8
化学文摘社编号:
分子量:
665.74
UNSPSC Code:
12352204
PubChem Substance ID:
MDL number:
InChI
1S/C33H43N7O8/c1-19-15-27(42)47-26-17-21(12-13-22(19)26)37-28(43)23(11-8-14-36-31(34)35)38-30(45)25(18-41)39-29(44)24(16-20-9-6-5-7-10-20)40-32(46)48-33(2,3)4/h5-7,9-10,12-13,15,17,23-25,41H,8,11,14,16,18H2,1-4H3,(H,37,43)(H,38,45)(H,39,44)(H,40,46)(H4,34,35,36)
SMILES string
CC1=CC(=O)Oc2cc(NC(=O)C(CCCNC(N)=N)NC(=O)C(CO)NC(=O)C(Cc3ccccc3)NC(=O)OC(C)(C)C)ccc12
InChI key
JLKJMNJZJBEYLQ-UHFFFAOYSA-N
assay
≥97% (TLC)
form
powder
solubility
DMSO: 20 mg/mL, clear, colorless to faintly yellow
storage temp.
−20°C
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
K Nakayama et al.
The Journal of biological chemistry, 270(40), 23619-23626 (1995-10-06)
Arginine-specific cysteine proteinase (Arg-gingipain; formerly, argingipain) is one of the major extracellular proteinases produced by the oral anaerobic bacterium Porphyromonas gingivalis. To determine whether Arg-gingipain is important for periodontopathogenicity of the organism, Arg-gingipain-deficient mutants were constructed via gene disruption by
L Fiorucci et al.
FEBS letters, 408(1), 85-88 (1997-05-12)
Tryptases are oligomeric enzymes localized in the secretory granules of mast cells. Their role(s) in vivo has yet to be clarified and the lack of powerful and specific inhibitors has hampered the comprehension of the biological functions of these enzymes.
Y Suzuki et al.
Archives of dermatological research, 285(6), 372-377 (1993-01-01)
In order to identify the endogenous protease associated with stratum corneum (SC) desquamation, we examined properties of proteases in the stratum corneum of normal human skin. SC were obtained by tape stripping, washed in toluene and then dried. The proteolytic
T Kambara et al.
Experientia, 42(2), 155-157 (1986-02-15)
Proteolytic enzymes of the guinea pig peritoneal exudate macrophages were investigated using synthetic fluorogenic peptide substrates. Among several enzymes, t-butyloxycarbonyl-phenylalanyl-seryl-arginine 4-methylcoumaryl-7-amide cleaving enzymes had the highest activity, and the activity in exudate macrophages was about 3 times stronger than that
N Fukusen et al.
Journal of biochemistry, 119(4), 633-638 (1996-04-01)
Novel trypsin-like serine proteases (mouse trypsin-type serine proteases 1 and 2 [MTSP-1 and -2]) were purified to homogeneity from mouse spleen. Each protease consisted of a single polypeptide with a molecular mass of about 29 kDa, as determined by sodium
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