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Merck

B6388

Sigma-Aldrich

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

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About This Item

Fórmula empírica (notación de Hill):
C33H43N7O8
Número de CAS:
Peso molecular:
665.74
Número MDL:
Código UNSPSC:
12352204
ID de la sustancia en PubChem:

Ensayo

≥97% (TLC)

Formulario

powder

solubilidad

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

temp. de almacenamiento

−20°C

cadena 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)

Clave InChI

JLKJMNJZJBEYLQ-UHFFFAOYSA-N

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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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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