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B6388

Sigma-Aldrich

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

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About This Item

Empirical Formula (Hill Notation):
C33H43N7O8
CAS Number:
73554-90-2
Molecular Weight:
665.74
MDL number:
MFCD00038451
UNSPSC Code:
12352204
PubChem Substance ID:
24891907

assay

≥97% (TLC)

form

powder

solubility

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

storage temp.

−20°C

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

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)

InChI key

JLKJMNJZJBEYLQ-UHFFFAOYSA-N

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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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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