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Item No. 37090
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Discover high-quality research tools to investigate GLP-1 mechanisms and next-generation metabolic targets.
OBESITY RESEARCH SOLUTIONSTransglutaminase 2 (TG2) is a calcium-dependent enzyme that is involved in a variety of biological activities.1,2 TG2 is composed of an N-terminal β sandwich containing integrin and fibronectin binding sites, a catalytic domain, a guanine nucleotide-binding site, and two C-terminal β-barrel domains.1 It is ubiquitously expressed and is localized to the cytosol, cytoskeleton, endoplasmic reticulum, mitochondria, nucleus, cell surface, and extracellular space in a context-dependent manner.3 TG2 catalyzes post-translational modifications of proteins via inter- or intramolecular crosslinking of glutamine and lysine residues or transamidation of glutamine residues with polyamines such as spermidine (Item No. 14918).1,2 It also exhibits calcium-independent enzyme activities, including GTPase, protein kinase, and disulfide isomerase activities, and binds to several cell surface adhesion molecules in the extracellular matrix (ECM).1,4 TG2 acts on a wide variety of protein substrates that have roles in neurological, autoimmune, and metabolic diseases, as well as carcinogenesis. Cayman’s Transglutaminase 2 Rabbit Monoclonal Antibody (Clone 013) can be used for ELISA.
WARNING This product is not for human or veterinary use.
1. Biological functionalities of transglutaminase 2 and the possibility of its compensation by other members of the transglutaminase family. ScientificWorldJournal 714561, (2014).
2. Mass spectrometric identification of the amino donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles. Biochemistry 30(12), 3114-3120 (1991).
3. Characterization of distinct sub-
4. Extracellular TG2: Emerging functions and regulation. FEBS J. 278(24), 4704-4716 (2011).