ANTIPAIN, DIHYDROCHLORIDE Property

Melting point:

209-217 °C

Boiling point:

652.92°C (rough estimate)

Density 

1.2423 (rough estimate)

refractive index 

1.6500 (estimate)

storage temp. 

-20°C

solubility 

H₂O: 50 mg/mL

form 

White powder

color 

White

Water Solubility 

0.01M in water

Stability:

Stable for 1 year from date of purchase as supplied. Solutions in distilled water may be stored at -20°C for up to 1 month.

Safety

Safety Statements 

22-24/25

WGK Germany 

3

RTECS 

YV9350800

F 

1-10

HS Code 

2934999090

Hazard and Precautionary Statements (GHS)

ANTIPAIN, DIHYDROCHLORIDE Chemical Properties,Usage,Production

Description

Antipain is a protease inhibitor originally isolated from actinomycetes. It inhibits thrombokinase, plasmin, trypsin, and papain in vitro (IC₅₀s = 20, 93, 0.26, and 0.16 μg/ml, respectively). Antipain (6-600 μg/ml) inhibits the morphological transformation of and increases frequency of chromosomal aberrations in Syrian hamster embryo cells induced by N-methyl-N''-nitro-N-nitroso-guanidine (MNNG). In vivo, antipain (25-100 mg/kg) suppresses urethan-induced formation of cleft palates and cleft lips in mice.

Uses

Concentrations for 50% inhibition (μg/ml): papain, 0.16trypsin, 0.26cathepsin A, 1.19cathepsin B, 0.59cathepsin D, 125plasmin, >93chymotrypsin and pepsin, >250It also has been reported to inhibit calpain I, (porcine) with Ki = 1.4 μM

Uses

Antipain inhibits trypsin, papain, and catherpsins A and B (a reversible inhibitor of cysteine and serine proteases). It is used to evaluate the role of proteases in cell transformations. It is used to help identify new proteases.

General Description

Antipain is a protease inhibitor isolated from actinomycetes. It inhibits thrombokinase and blood coagulation.

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 of antipain can reduce the frequency of chemically induced transformation in BALB/c-/3T3 cells.

References

1) Umezawa?et al.?(1976),?Structures and activities of protease inhibitors of microbial origin; Method Enzymol.,?45?678 2) Gotoh?et al.?(2001),?Proteolytic activity and recombinant protein production in virus-infected Sf-9 insect cell cultures supplemented with carboxyl and cysteine protease inhibitors; J. Biosci. Bioeng.,?92?248 3) Hockensmith?et al. (2016), Identification and characterization of a chymotrypsin-like serine protease from periodontal pathogen, Tannerella forsythia; Microb. Pathog.,?100?37 4) Mat Amin?et al. (2004),?Proteinases in Naegleria Fowleri (strain NF3), a pathogenic amoeba: a preliminary study.; Trop. Biomed.,?21?57 5) Moriyyasu & Inoue (2008),?Use of protease inhibitor for detecting autophagy in plants; Methods Enzymol.,?451?557