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B6388

Sigma-Aldrich

Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin

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About This Item

Formule empirique (notation de Hill):
C33H43N7O8
Numéro CAS:
73554-90-2
Poids moléculaire :
665.74
Numéro MDL:
MFCD00038451
Code UNSPSC :
12352204
ID de substance PubChem :
24891907

Pureté

≥97% (TLC)

Forme

powder

Solubilité

DMSO: 20 mg/mL, clear, colorless to faintly yellow

Température de stockage

−20°C

Chaîne SMILES 

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

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)

Clé InChI

JLKJMNJZJBEYLQ-UHFFFAOYSA-N

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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Consulter la Bibliothèque de documents

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
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
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.
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
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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