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AEBSF.HClSerine protease inhibitor

AEBSF.HCl

Catalog No. A2573
Size Price Stock Qty
10mM (in 1mL DMSO) $55.00 In stock
100mg $56.00 In stock
500mg $200.00 In stock

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Sample solution is provided at 25 µL, 10mM.

Quality Control

Chemical structure

AEBSF.HCl

Related Biological Data

AEBSF.HCl

Related Biological Data

AEBSF.HCl

Biological Activity

Description AEBSF.HCl is an irreversible broad spectrum inhibitor of serine protease.
Targets serine protease          
IC50            

Protocol

Cell experiment [1]:

Cell lines

K695sw, HS695 and SKN695 cells

Preparation method

The solubility of this compound in DMSO is >10 mM. General tips for obtaining a higher concentration: Please warm the tube at 37℃ for 10 minutes and/or shake it in the ultrasonic bath for a while. Stock solution can be stored below -20℃ for several months.

Reaction Conditions

0, 0.1, 0.3, 0.6, 0.8, 1.0 and 1.2 mM; 20 mins

Applications

AEBSF was found to inhibit Aβ production in various cell lines. In K293 cells transfected with βAPP695 (K695sw), AEBSF showed dose-dependent reduction of Aβ with the IC50 value of about 1 mM. In HS695 and SKN695 cells transfected with wild-type APP695, AEBSF showed inhibition effect with IC50 value of about 300 μM. AEBSF was also found to increase α-cleavege and inhibit β- cleavage.

Animal experiment [2]:

Animal models

SD rats

Dosage form

Intrauterine (5 mg or 10 mg AEBSF per injection) or tail vein (10 mg AEBSF per rat) administration on day 3 of pregnancy

Applications

According to the number of visible implanted embryos on day 8 of pregnancy, it was shown that AEBSF inhibited embryo implantation in rat.

Other notes

Please test the solubility of all compounds indoor, and the actual solubility may slightly differ with the theoretical value. This is caused by an experimental system error and it is normal.

References:

[1]. Citron M, Diehl T S, Capell A, et al. Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF. Neuron, 1996, 17(1): 171-179.

[2]. Jiang YH, Shi Y, He YP, Du J, Li RS, Shi HJ, Sun ZG, Wang J. Serine protease inhibitor 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride (AEBSF) inhibits the rat embryo implantation in vivo and interferes with cell adhesion in vitro. Contraception. 2011 Dec;84(6):642-8.

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Chemical Properties

Cas No. 30827-99-7 SDF Download SDF
Synonyms AEBSF.HCl,AEBSF Hydrochloride
Chemical Name 4-(2-aminoethyl)benzenesulfonyl fluoride;hydrochloride
Canonical SMILES C1=CC(=CC=C1CCN)S(=O)(=O)F.Cl
Formula C8H10FNO2S.HCl M.Wt 239.69
Solubility >12mg/mL in DMSO Storage Desiccate at -20°C
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
Shipping Condition Evaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request

Background

AEBSF is a broad spectrum, irreversible inhibitor of serine proteases [1].

AEBSF is a covalently binding inhibitor of proteases, including trypsin, chymotrypsin, plasmin and thrombin. AEBSF was found to inhibit Aβ production in various cell lines. In K293 cells transfected with APP695 (K695sw), AEBSF showed does-dependent reduction of Aβ with IC50 value of about 1mM. In HS695 and SKN695 cells transfected with wild-type APP695, AEBSF showed inhibition effect with IC50 value of about 300 μM. AEBSF was also found to increase α-cleavege and inhibit β- cleavage. Besides that, as a protease inhibitor, AEBSF was reported to prevent monocyte-derived macrophages from lysing the leukemic cells. Incubation of macrophages with 150 μM AEBSF for 6 hours resulted in nearly maximum inhibition [1, 2].

References:
[1] Citron M, Diehl T S, Capell A, et al. Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF. Neuron, 1996, 17(1): 171-179.
[2] Nakabo Y, Pabst M J. Lysis of leukemic cells by human macrophages: inhibition by 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), a serine protease inhibitor. Journal of leukocyte biology, 1996, 60(3): 328-336.