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Key Documents

SML2490

Sigma-Aldrich

APC366 trifluoroacetate

≥97% (HPLC)

Synonyme(s) :

APC 366 trifluoroacetate, N-(1-Hydroxy-2-naphthoyl)-L-arginyl-L-prolinamide, N2-[(1-Hydroxy-2-naphthalenyl)carbonyl]-L-arginyl-L-prolinamide trifluoroacetate

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About This Item

Formule empirique (notation de Hill):
C22H28N6O4 · xC2HF3O2
Numéro CAS:
Poids moléculaire :
440.50 (free base basis)
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77

Pureté

≥97% (HPLC)

Forme

lyophilized powder

Couleur

white to off-white

Conditions d'expédition

wet ice

Température de stockage

−20°C

Chaîne SMILES 

FC(F)(C(O)=O)F.NC(NCCC[C@@H](C(N1CCC[C@H]1C(N)=O)=O)NC(C2=C(O)C3=CC=CC=C3C=C2)=O)=N

InChI

1S/C22H28N6O4/c23-19(30)17-8-4-12-28(17)21(32)16(7-3-11-26-22(24)25)27-20(31)15-10-9-13-5-1-2-6-14(13)18(15)29/h1-2,5-6,9-10,16-17,29H,3-4,7-8,11-12H2,(H2,23,30)(H,27,31)(H4,24,25,26)/t16-,17-/m0/s1

Clé InChI

SKYWIMYOGAWOMB-IRXDYDNUSA-N

Actions biochimiques/physiologiques

APC366 is a selective inhibitor of mast cell tryptase, which is involved with allergenic response. It thereby also inhibits protease-activated receptor PAR2, a G-protein-coupled receptor that is activated by mast cell tryptase. Tryptase has been proposed to be involved in fibrosis, joint inflammation and also in promoting breast cancer angiogenesis, all of which APC366 inhibited.

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Consulter la Bibliothèque de documents

Issan Yee San Tam et al.
International archives of allergy and immunology, 177(3), 199-206 (2018-07-19)
Mast cells are key immune effector cells which release chemokines, proteases, and other inflammatory mediators upon activation by immunological stimuli. The aim of this study was to investigate the effects of co-releasing proteases on the kinetics of release of the
Neng Qian et al.
Oncology letters, 16(2), 1513-1520 (2018-07-17)
Mast cells have been demonstrated to accumulate around and within solid tumors of numerous types, and express a number of pro-angiogenic compounds, including tryptase. They may serve an early role in angiogenesis within developing tumors. In the present study, the
Alexandre Denadai-Souza et al.
Arthritis research & therapy, 19(1), 124-124 (2017-06-08)
Increasing evidences indicate that an unbalance between tryptases and their endogenous inhibitors, leading to an increased proteolytic activity, is implicated in the pathophysiology of rheumatoid arthritis. The aim of the present study was to evaluate the impact of tryptase inhibition

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