Back to all products
| Factor XIII |
| Transglutaminase 1 |
| Transglutaminase 2 |
| Transglutaminase 3 |
| Transglutaminase 4 |
| Transglutaminase 5 |
| Transglutaminase 6 |
| Transglutaminase 7 |
| Microbial TGase |
Transglutaminases
The history of the enzyme class of transglutaminases started almost 60 years ago, when the term transglutaminase (TG) was introduced in scientific literature by Heinrich Waelsch and coworkers.
Today, we know that we are talking about a family of nine different isoenzymes in the human body. Although transglutaminases have one basic common feature – the formation of high molecular weight aggregates by covalent protein cross-linking – they fulfill a plentitude of other catalytic and physiological functions.
The sketch below gives you a rough overview about the transglutaminase family members and their implications in physiology, diseases and diagnostics - as it is known today.
Successful ISO9001:2015 recertification 
Dr. Falk Pharma and Zedira announce successful completion of the phase 2a proof-of-concept study of ZED1227 for the treatment of Celiac Disease 
Dr. Falk Pharma und Zedira verkünden den erfolgreichen Abschluss der Phase 2a-Studie mit ZED1227 zur Behandlung von Zöliakie 
Reversibly acting transglutaminase 2 inhibitors: drug candidates for the treatment of fibrosis 
Transglutaminase antibodies and neurological manifestations of gluten sensitivity 
Design of Oral FXIIIa Blockers as Safer Anticoagulants Mission Impossible? 
Microbial transglutaminase (MTG) enables efficient and site-specific conjugation to native antibodies without the need of antibody engineering 
Tridegin as FXIIIa inhibitor 
Microbial transglutaminase: from discovery to market 
Tissue transglutaminase inhibitors 
Tissue transglutaminase in Alzheimers Disease 
Factor XIIIa: novel target for anticoagulation? 
Microbial transglutaminase for site-specific protein conjugation