human Factor XIIIa, Thrombin-activated, recombinant

Description
Human Factor XIII was recombinantly produced in insect cells. Factor XIII is a homodimer (a₂) composed of two chains held together by non-covalent bonds. After activation of the zymogen by Thrombin and Ca²⁺ to its active form (a*₂ , Factor XIIIa), Factor XIIIa catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. The resulting cross-linked fibrin is insoluble and resistant to lysis.

Synonym    
Recombinant Fibrin stabilizing factor, protein-glutamine-γ-glutamyltransferase    

Purity > 95% [by SDS-PAGE]

Molecular Weight  79 kDa (monomer)
                                 158 kDa (homodimer)

Application    
The FXIIIa catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue.

Presentation    
200 µg of the recombinant activated human Factor XIIIa is lyophilized from 50 mM Tris-HCl pH 8.0, 300 mM NaCl, 1 mM CHAPS, 3 mM Ca2+. Sample contains sucrose.

Reconstitution    
Add the volume of water specified in the certificate of analysis under aliquotation to the vial of lyophilized powder. Rotate vial gently until solid dissolves. After reconstitution the solution should be stored frozen in working aliquots. For short term storage keep cooled on ice.

Storage    
Store at –20 °C in working aliquots. Repeated freezing and thawing is not recommended.
Delivery at ambient temperature is possible

Category: Research use only

Type: Protein

Product Availability: Worldwide

Manufacturer: ImmBioMed GmbH & Co KG, German

References    

1. The blood clotting Factor XIIIa forms unique complexes with amyloid-beta (Aβ) and colocalizes with deposited Aβ in cerebral amyloid angiopathy. de Jager M et al. Neuropathol Appl Neurobiol. 2016 Apr;42(3):255-72.
2. Novel insights into structure and function of factor XIIIa-inhibitor tridegin. Böhm M et al. J Med Chem. 2014 Dec 26;57(24):10355-65.