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B9385

Sigma-Aldrich

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

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135,00 €

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135,00 €

About This Item

Formula empirica (notazione di Hill):
C31H45N7O7
Numero CAS:
70375-24-5
Peso molecolare:
627.73
Numero MDL:
MFCD00058181
Codice UNSPSC:
12352204
ID PubChem:
24892134
NACRES:
NA.32

135,00 €

Per informazioni sulla disponibilità, contatta il Servizio Clienti.

Saggio

≥98% (TLC)

Stato

powder

Solubilità

water: 20 mg/mL, clear, colorless

Temperatura di conservazione

−20°C

Stringa SMILE

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
ROQGJTZGLVLVIN-UHFFFAOYSA-N

Descrizione generale

Boc-Val-Pro-Arg-AMC serves as a synthetic substrate for human kallikrein 8.[1]

Applicazioni

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[2]
  • as a fluorogenic substrate for thrombin in inhibitory assay with recombinant E. nipponicum serpin[3]
  • as a substrate in proteinase assay with hemolymph protein[4]

Confezionamento

Bottomless glass bottle. Contents are inside inserted fused cone.

Substrati

A fluorogenic substrate for thrombin.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
BCCM4330
BCCL2939
BCCK3625
BCCH2497
BCCG1065

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

Sigma-Aldrich

T6884

Trombina

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

Sigma-Aldrich

T9326

Thrombin human

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
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
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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Protocolli

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.

Domande

Recensioni

Nessuna valutazione

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