Human Factor XIa – blocked active site (EGRck)

< 1 % activity XIa - Active-site blocked
MW(Da) : 160 000
Extinction coef. : 13.4
 

EGRck (or Glu-Gly-Arg chloromethyl ketone) is an irreversible serine protease inhibitor designed to target enzymes that recognize the Glu-Gly-Arg amino acid sequence.

More specifically:

• Full name: Glutamyl-Glycyl-Arginyl chloromethyl ketone
• Abbreviation: EGRck
• Molecule type: Peptide chloromethyl ketone

Mechanism of action

The chloromethyl ketone (CMK) group is highly reactive and forms a covalent bond with the active-site histidine residue of serine proteases. This results in:

• irreversible enzyme inactivation;
• permanent loss of catalytic activity.

Target enzymes

EGRck is primarily used to inhibit serine proteases with specificity for basic amino acid residues, including:

• Coagulation factor VIIa (under certain experimental conditions),
• Coagulation factor IXa,
• Coagulation factor Xa,
• and other trypsin-like serine proteases, depending on their substrate specificity.

Research applications

EGRck is commonly used to:

• selectively inhibit serine proteases in biological samples;
• investigate blood coagulation mechanisms;
• identify proteases involved in specific biological pathways;
• stabilize protein preparations by preventing proteolytic degradation.

The vast majority of enzymes is pure (without additives) with > 95% purity SDS-PAGE.
Expiration date of one year from delivery.
Delivery in large quantities.
Discount according to quantities.

An enzyme is a protein that catalyzes a biochemical reaction. It converts a substrate into a product. Each enzyme has a structure adapted to its function and its activity is dependent on an optimum temperature and pH.
Factor XI (FXI) is a protein synthesized by the liver. It participates in the contact phase which initiates the intrinsic pathway of coagulation.
It is activated by FXIIa to factor FXIa which will itself activate FIX in the presence of calcium ions.

EGRck :Glu-Gly-Arg chloromethyl ketone. MW : 466 g/mol