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10791

Sigma-Aldrich

Antipain

>50000 U/mg

Synonym(s):

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

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5 MG
$130.00
25 MG
$463.00

$130.00

Estimated to ship onMarch 21, 2025

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5 MG
$130.00
25 MG
$463.00

About This Item

Empirical Formula (Hill Notation):
C27H44N10O6
CAS Number:
37691-11-5
Molecular Weight:
604.70
Beilstein/REAXYS Number:
6837629
EC Number:
253-631-0
MDL number:
MFCD00135959
UNSPSC Code:
12352202
PubChem Substance ID:
57646816
NACRES:
NA.77

$130.00

Estimated to ship onMarch 21, 2025

Quality Level

100

specific activity

>50000 U/mg

mode of action

enzyme | inhibits

storage temp.

−20°C

SMILES string

[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

InChI key

SDNYTAYICBFYFH-KTYMLHDXSA-N

General description

Chemical structure: peptide

Biochem/physiol Actions

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.[1]
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.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

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)

Other Notes

Protease inhibitor[2]

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
BCCK3619
BCCH3240
BCCF9432
BCCD7591
BCCB7413

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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
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
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
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
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