Skip to Content
Merck
All Photos(1)

Documents

Safety Information

101500

Sigma-Aldrich

AEBSF, Hydrochloride

AEBSF, CAS 30827-99-7, is a specific irreversible inhibitor of chymotrypsin, kallikrein, plasmin, thrombin, trypsin, and related thrombolytic enzymes. A nontoxic alternative to PMSF and DFP.

Synonym(s):

AEBSF, Hydrochloride

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

Empirical Formula (Hill Notation):
C8H10FNO2S · xHCl
CAS Number:
30827-99-7
Molecular Weight:
203.23 (free base basis)
MDL number:
MFCD00132962
UNSPSC Code:
12352202
NACRES:
NA.77

Quality Level

100

Assay

>97% (HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated

color

white to off-white

solubility

water: 25 mg/mL

shipped in

ambient

storage temp.

−20°C

InChI

1S/C8H10FNO2S.ClH/c9-13(11,12)8-3-1-7(2-4-8)5-6-10;/h1-4H,5-6,10H2;1H

InChI key

WRDABNWSWOHGMS-UHFFFAOYSA-N

General description

AEBSF, CAS 30827-99-7, is a specific irreversible inhibitor of chymotrypsin, kallikrein, plasmin, thrombin, trypsin, and related thrombolytic enzymes. A nontoxic alternative to PMSF and DFP.
Specific irreversible inhibitor of serine proteases. Reacts covalently with a serine at the active site. Inhibits chymotrypsin, kallikrein, plasmin, thrombin, trypsin, and related thrombolytic enzymes. Stable, nontoxic alternative to PMSF (Cat. No. 52332) and DFP (Cat. No. 30967). Used at the same molar concentration (0.1-1.0 mM) as PMSF for most applications. Exhibits low inhibitory activity towards proteinase K.
Specific, irreversible inhibitor of serine proteases. Inhibits chymotrypsin, kallikrein, plasmin, thrombin, trypsin, and related thrombolytic enzymes. Stable, nontoxic alternative to PMSF (Cat. No. 52332) and DFP (Cat. No. 30967). A β-secretase inhibitor that inhibits β-amyloid peptide (Aβ) production and enhances amyloid precursor protein (sAPPUα) secretion in several cell lines at millimolar concentrations. Use at the same molar concentrations (0.1-1.0 mM) as PMSF for most applications. Also available as a 50 mM solution in H2O (Cat. No. 508436).

Biochem/physiol Actions

Primary Target
chymotrypsin
Product does not compete with ATP.

Packaging

Packaged under inert gas

Warning

Toxicity: Standard Handling (A)

Reconstitution

Following reconstitution, store in the refrigerator (4°C). Aqueous stock solutions are stable for up to 2 months at 4°C. Slight hydrolysis occurs at alkaline pH (8-9).

Other Notes

Citron, M., et al. 1996. Neuron 17, 171.
Ohkubo, I., et al. 1994. J. Biochem. 116, 1182.
Mintz, G.R. 1993. BioPharm. 6, 34.
Lawson, W.B., et al. 1982. Folia Haematol.109, 52.
Markwardt, F., et al. 1974. Biochem. Pharmacol.23, 2247.
Markwardt, F., et al. 1973. Thromb. Res.2, 343.
Baker, B.R., and Cory, M. 1971. J. Med. Chem.14, 119.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictograms

Corrosion
GHS05

Signal Word

Danger

Hazard Statements

H314

Hazard Classifications

Eye Dam. 1 - Skin Corr. 1A

Storage Class Code

8A - Combustible corrosive hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

101500-5GM:
101500-6GM:
101500-500MG:
101500-VMG:
101500-50MG:
101500-1GM:
101500-100MG:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Natarajan V Bhanu et al.
Bio-protocol, 10(18), e3756-e3756 (2021-03-05)
Chromatin modifications, like histone post translational modifications (PTMs), are critical for tuning gene expression and many other aspects of cell phenotype. Liquid chromatography coupled to mass spectrometry (LC-MS) has become the most suitable method to analyze histones and histone PTMs
Michael C Yoon et al.
Biochemistry, 62(15), 2289-2300 (2023-07-17)
The biological and pathological functions of cathepsin B occur in acidic lysosomes and at the neutral pH of cytosol, nuclei, and extracellular locations. Importantly, cathepsin B displays different substrate cleavage properties at acidic pH compared to neutral pH conditions. It
Ziyi Liu et al.
Methods and protocols, 7(1) (2024-02-23)
The development of monoclonal antibodies (mAbs) represents a significant milestone in both basic research and clinical applications due to their target specificity and versatility in therapeutic and diagnostic applications. The innovative strategy of mAb screening, utilizing phage display, facilitates the
Hailing Shi et al.
Nature, 622(7983), 552-561 (2023-09-28)
Spatially charting molecular cell types at single-cell resolution across the 3D volume is critical for illustrating the molecular basis of brain anatomy and functions. Single-cell RNA sequencing has profiled molecular cell types in the mouse brain1,2, but cannot capture their
Navid Paknejad et al.
Nature communications, 14(1), 6897-6897 (2023-10-29)
Inositol 1,4,5-trisphosphate receptors (IP3Rs) are endoplasmic reticulum Ca2+ channels whose biphasic dependence on cytosolic Ca2+ gives rise to Ca2+ oscillations that regulate fertilization, cell division and cell death. Despite the critical roles of IP3R-mediated Ca2+ responses, the structural underpinnings of
View All Related Papers

Articles

YeastBuster™ Protein Extraction Reagent for Fast, Efficient Extraction of Proteins from Yeast

YeastBuster™ Protein Extraction Reagent for Fast, Efficient Extraction of Proteins from Yeast

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service