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Merck

A6191

Sigma-Aldrich

Antipain dihydrochloride

lyophilized powder

Sinónimos:

N-(Nα-Carbonyl-Arg-Val-Arg-al)-Phe

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About This Item

Fórmula empírica (notación de Hill):
C27H44N10O6 · 2 HCl
Número de CAS:
Peso molecular:
677.62
Número MDL:
Código UNSPSC:
12352202
ID de la sustancia en PubChem:
NACRES:
NA.77

product name

Antipain dihydrochloride from microbial source, protease inhibitor

origen biológico

Streptomyces sp.

Nivel de calidad

formulario

lyophilized powder

potencia

1.4 μM Ki

solubilidad

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

Modo de acción

enzyme | inhibits

temp. de almacenamiento

−20°C

cadena 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

Clave InChI

YAHXZYICKJUJEO-BXLPLHKWSA-N

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Descripción general

Chemical structure: peptide

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Nota de preparación

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.

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)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Dawson, R., ed.
Data for Biochemical Research, 328-328 (1987)
Methods for Protein Analysis: A Practical Guide for Laboratory Protocols, 23-23 (2013)
Beynon, R.J. and Bond, J.S., ed.
Proteolytic Enzymes: A Practical Approach, 242-242 (1989)
The adipose tissue phenotype of hormone-sensitive lipase deficiency in mice
Wang S, et al.
Obesity Research, 9(2), 119-128 (2001)
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

Artículos

Papain is a cysteine protease of the peptidase C1 family. Papain consists of a single polypeptide chain with three disulfide bridges and a sulfhydryl group necessary for activity of the enzyme.

Contenido relacionado

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

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