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Documentos Principais

10791

Sigma-Aldrich

Antipain

>50000 U/mg

Sinônimo(s):

[(S)-1-Carboxy-2-phenylethyl]carbamoyl-L-arginyl-L-valyl-argininal

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About This Item

Fórmula empírica (Notação de Hill):
C27H44N10O6
Número CAS:
Peso molecular:
604.70
Beilstein:
6837629
Número CE:
Número MDL:
Código UNSPSC:
12352202
ID de substância PubChem:
NACRES:
NA.77

atividade específica

>50000 U/mg

Modo de ação

enzyme | inhibits

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

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

InChI

1S/C27H44N10O6/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)/t18?,19-,20-,21-/m0/s1

chave InChI

SDNYTAYICBFYFH-KTYMLHDXSA-N

Categorias relacionadas

Descrição geral

Chemical structure: peptide

Ações bioquímicas/fisiológicas

Inhibits serine/cysteine proteases and some trypsin-like proteases. Compare activity to that of leupeptin. Used to evaluate the role of proteases in cell transformations. Used to help identify new proteases.
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 can reduce the frequency of chemically induced transformation in BALB/c-/3T3 cells.

Embalagem

Bottomless glass bottle. Contents are inside inserted fused cone.

Definição da unidade

1 U corresponds to the amount of inhibitor which reduces the trypsin activity by 1 BAEE-U. (1 BAEE-U is the amount of enzyme which increases the absorbance at 253 nm by 0.001 per minute at pH 7.6 and 25°C; BAEE, Cat. No. 12880, as substrate)

Outras notas

Protease inhibitor

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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Sigma-Aldrich

77170

Pepstatina A

Leupeptina powder, from synthetic, =96.5%

Roche

LEU-RO

Leupeptina

E-64 protease inhibitor

Sigma-Aldrich

E3132

E-64

Pepstatina A from Streptomyces species

Roche

PEPS-RO

Pepstatina A

Pepstatina A microbial, ≥75% (HPLC)

Sigma-Aldrich

P4265

Pepstatina A

Catherine Gaitanaki et al.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 13(3), 173-180 (2003-07-24)
To examine whether the calpain-calpastatin system is activated during the calcium paradox in the isolated perfused pigeon heart, we separated the protease from its inhibitor calpastatin and studied its kinetic properties. The protease exhibits kinetic properties similar to those of
Tanya V Kogan et al.
The Journal of infectious diseases, 189(11), 1965-1973 (2004-05-15)
Aspergillus fumigatus is an opportunistic pathogenic fungus that predominantly infects the respiratory system. Penetration of the lung alveolar epithelium is a key step in the infectious process. The cytoskeleton of alveolar epithelial cells forms the cellular basis for the formation
E S Johnson et al.
The Journal of cell biology, 147(5), 981-994 (1999-12-01)
SUMO is a ubiquitin-related protein that functions as a posttranslational modification on other proteins. SUMO conjugation is essential for viability in Saccharomyces cerevisiae and is required for entry into mitosis. We have found that SUMO is attached to the septins
Raquel Alves Dos Santos et al.
Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association, 46(2), 671-677 (2007-10-27)
The use of antioxidants during chemotherapy has been shown to reduce or prevent the undesirable effects experienced by healthy cells. Micronutrient selenium is well known for its antioxidant properties; however, selenium exhibits a bimodal nature in that both its beneficial
André L S Santos et al.
International journal for parasitology, 36(1), 47-56 (2005-11-29)
In this study, we report the ultrastructural and growth alterations caused by cysteine peptidase inhibitors on the plant trypanosomatid Phytomonas serpens. We showed that the cysteine peptidase inhibitors at 10 microM were able to arrest cellular growth as well as

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