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B9385

Sigma-Aldrich

Boc-Val-Pro-Arg-7-amido-4-methylcoumarin hydrochloride

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About This Item

Fórmula empírica (notación de Hill):
C31H45N7O7
Número de CAS:
70375-24-5
Peso molecular:
627.73
Número MDL:
MFCD00058181
Código UNSPSC:
12352204
ID de la sustancia en PubChem:
24892134
NACRES:
NA.32

Ensayo

≥98% (TLC)

Nivel de calidad

200

Formulario

powder

solubilidad

water: 20 mg/mL, clear, colorless

temp. de almacenamiento

−20°C

cadena SMILES

Cl.CC(C)C(NC(=O)OC(C)(C)C)C(=O)N1CCCC1C(=O)NC(CCCNC(N)=N)C(=O)Nc2ccc3C(C)=CC(=O)Oc3c2

InChI

1S/C31H45N7O7.ClH/c1-17(2)25(37-30(43)45-31(4,5)6)28(42)38-14-8-10-22(38)27(41)36-21(9-7-13-34-29(32)33)26(40)35-19-11-12-20-18(3)15-24(39)44-23(20)16-19;/h11-12,15-17,21-22,25H,7-10,13-14H2,1-6H3,(H,35,40)(H,36,41)(H,37,43)(H4,32,33,34);1H

Clave InChI

ROQGJTZGLVLVIN-UHFFFAOYSA-N

Descripción general

Boc-Val-Pro-Arg-AMC serves as a synthetic substrate for human kallikrein 8.

Aplicación

Boc-Val-Pro-Arg-7-amido-4-methylcoumarin hydrochloride has been used:
  • as a fluorogenic substrate for thrombin in inhibitory assay with salivary protein cE5
  • as a fluorogenic substrate for thrombin in inhibitory assay with recombinant E. nipponicum serpin
  • as a substrate in proteinase assay with hemolymph protein

Envase

Bottomless glass bottle. Contents are inside inserted fused cone.

Sustratos

A fluorogenic substrate for thrombin.

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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Certificados de análisis (COA)

Lot/Batch Number
BCCM4330
BCCL2939
BCCK3625
BCCH2497
BCCG1065

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Trombina from human plasma lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280, 18.3)

Sigma-Aldrich

T6884

Trombina from human plasma

Thrombin human BioUltra, recombinant, expressed in HEK 293 cells, aqueous solution, ≥95% (SDS-PAGE)

Sigma-Aldrich

T9326

Thrombin human

Tadaaki Kishi et al.
Biological chemistry, 387(6), 723-731 (2006-06-28)
Human kallikrein 8 (hK8), whose gene was originally cloned as the human ortholog of a mouse brain protease, is known to be associated with diseases such as ovarian cancer and Alzheimer's disease. Recombinant human pro-kallikrein 8 was activated with lysyl
Luciano Pirone et al.
The Journal of biological chemistry, 292(30), 12632-12642 (2017-06-09)
Saliva of blood-feeding arthropods carries several antihemostatic compounds whose physiological role is to facilitate successful acquisition of blood. The identification of novel natural anticoagulants and the understanding of their mechanism of action may offer opportunities for designing new antithrombotics disrupting
Jantiwan Sutthangkul et al.
The Journal of biological chemistry, 290(10), 6470-6481 (2015-01-13)
The melanization cascade, activated by the prophenoloxidase (proPO) system, plays a key role in the production of cytotoxic intermediates, as well as melanin products for microbial sequestration in invertebrates. Here, we show that the proPO system is an important component
Pavel Roudnický et al.
Parasite (Paris, France), 25, 61-61 (2018-12-06)
Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in
T Morita et al.
Journal of biochemistry, 82(5), 1495-1498 (1977-11-01)
Twenty peptide-4-methylcoumarin amides (MCA) were newly synthesized and tested as possible substrates for alpha-thrombin, factor Xa, kallikreins, urokinase, and plasmin. These fluorogenic peptides contained arginine-MCA as the carboxyl-terminus. Release of 7-amino-4-methylcoumarin was determined fluorometrically. Of these peptides, the following were
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Protocolos

Thrombin from Bovine Plasma

Thrombin is an endolytic serine protease that selectively cleaves the Arg–Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

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