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Merck

A6191

Sigma-Aldrich

Antipain dihydrochloride

lyophilized powder

Synonim(y):

N-(Nα-Carbonyl-Arg-Val-Arg-al)-Phe

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About This Item

Wzór empiryczny (zapis Hilla):
C27H44N10O6 · 2 HCl
Numer CAS:
Masa cząsteczkowa:
677.62
Numer MDL:
Kod UNSPSC:
12352202
Identyfikator substancji w PubChem:
NACRES:
NA.77

product name

Antipain dihydrochloride from microbial source, protease inhibitor

pochodzenie biologiczne

Streptomyces sp.

Poziom jakości

Postać

lyophilized powder

siła działania

1.4 μM Ki

rozpuszczalność

H2O: 50 mg/mL
1-butanol: soluble
1-propanol: soluble
DMSO: soluble
ethanol: soluble
methanol: soluble

Tryb działania

enzyme | inhibits

temp. przechowywania

−20°C

ciąg SMILES

Cl[H].Cl[H].[H]C(=O)C(CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)NC(Cc1ccccc1)C(O)=O)C(C)C

InChI

1S/C27H44N10O6.2ClH/c1-16(2)21(23(40)34-18(15-38)10-6-12-32-25(28)29)37-22(39)19(11-7-13-33-26(30)31)35-27(43)36-20(24(41)42)14-17-8-4-3-5-9-17;;/h3-5,8-9,15-16,18-21H,6-7,10-14H2,1-2H3,(H,34,40)(H,37,39)(H,41,42)(H4,28,29,32)(H4,30,31,33)(H2,35,36,43);2*1H/t18?,19-,20?,21-;;/m0../s1

Klucz InChI

YAHXZYICKJUJEO-BXLPLHKWSA-N

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Opis ogólny

Chemical structure: peptide

Zastosowanie

Antipain dihydrochloride from microbial source has been used in the preparation of adipocyte proteins for western blotting and in protease inhibitor cocktail for isolating nuclear extracts for gelshift analysis.
Concentrations for 50% inhibition (μg/ml):
papain, 0.16
trypsin, 0.26
cathepsin A, 1.19
cathepsin B, 0.59
cathepsin D, 125
plasmin, >93
chymotrypsin and pepsin, >250
It also has been reported to inhibit calpain I, (porcine) with Ki = 1.4 μM

Działania biochem./fizjol.

Antipain dihydrochloride also inhibits the action of papain and cathespsin B.
Reversible inhibitor of serine/cysteine proteases and some trypsin-like serine proteases. Its action resembles leupeptin; however, its plasmin inhibition is less and its cathepsin A inhibition is more than that observed with leupeptin. Chronic administration of antipain can reduce the frequency of chemically induced transformation in BALB/c-/3T3 cells.

Uwaga dotycząca przygotowania

Solubility testing at 50 mg/ml in water yields a clear to slightly hazy yellow solution. It is reportedly soluble in methanol, water, and DMSO; less soluble in ethanol, butanol, and propanol; insoluble in benzene, hexane, and chloroform.8 A stock solution in water or buffer is stable for about a month at -20 °C.

Dilute solutions should be stored on ice and kept for only a day because of the terminal aldehyde, which is subject to oxidation and racemization.
Stock solutions in water or buffer stable for 1 week at 4 °C, 1 month at −20 °C.
This page may contain text that has been machine translated.

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

The adipose tissue phenotype of hormone-sensitive lipase deficiency in mice
Wang S, et al.
Obesity Research, 9(2), 119-128 (2001)
Dawson, R., ed.
Data for Biochemical Research, 328-328 (1987)
Wenjie Xia et al.
Foods (Basel, Switzerland), 9(6) (2020-07-02)
In this study, a novel method called selective proteolysis was applied to the glycinin component of soy protein isolate (SPI), and a degraded glycinin hydrolysate (DGH) was obtained. The effects of high-intensity ultrasound (HIU) treatment (20 kHz at 400 W
Zollner, H., ed.
Handbook of Enzyme Inhibitors, 94-94 (1993)
Mechanism of interferon-gamma mediated down-regulation of interleukin-10 gene expression
Schaefer A, et al.
Molecular Immunology, 46(7), 1351-1359 (2009)

Produkty

Uncover properties and applications of the cysteine protease papain and find inhibitors, substrates, and other papain products.

Protokoły

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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