TGM2/Transglutaminase 2 Protein, Mouse (His)

TGM2/Transglutaminase 2 protein, a calcium-dependent acyltransferase, catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, leading to the cross-linking or amination of proteins. Involved in diverse biological processes such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification, and apoptosis, TGM2 acts as a protein-glutamine gamma-glutamyltransferase. It mediates the cross-linking of proteins, including ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1, and WDR54. The protein cross-linking activity is inhibited under physiological conditions by GTP, and this inhibition is relieved by Ca(2+) in response to various stresses. In addition to its role in apoptosis by promoting cytoskeletal protein cross-linking and mediating the formation of extracellular matrix scaffolds, TGM2 can use monoamine substrates to catalyze diverse protein post-translational modifications. It plays a crucial role in chromatin organization by mediating serotonylation and dopaminylation of histone H3, contributing to neurotransmission-independent functions in ventral tegmental area (VTA) neurons. Furthermore, TGM2 acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity, highlighting its involvement in signaling pathways beyond its acyltransferase activity. TGM2/Transglutaminase 2 Protein, Mouse (His) is the recombinant mouse-derived TGM2/Transglutaminase 2 protein, expressed by E. coli , with N-His labeled tag. The total length of TGM2/Transglutaminase 2 Protein, Mouse (His) is 685 a.a., with molecular weight of ~78.2 kDa.

TGM2/Transglutaminase 2 protein, a calcium-dependent acyltransferase, catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, leading to the cross-linking or amination of proteins. Involved in diverse biological processes such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification, and apoptosis, TGM2 acts as a protein-glutamine gamma-glutamyltransferase. It mediates the cross-linking of proteins, including ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1, and WDR54. The protein cross-linking activity is inhibited under physiological conditions by GTP, and this inhibition is relieved by Ca(2+) in response to various stresses. In addition to its role in apoptosis by promoting cytoskeletal protein cross-linking and mediating the formation of extracellular matrix scaffolds, TGM2 can use monoamine substrates to catalyze diverse protein post-translational modifications. It plays a crucial role in chromatin organization by mediating serotonylation and dopaminylation of histone H3, contributing to neurotransmission-independent functions in ventral tegmental area (VTA) neurons. Furthermore, TGM2 acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity, highlighting its involvement in signaling pathways beyond its acyltransferase activity.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Mouse

E. coli

N-His

P21981 (A2-A686)

21817  [NCBI]

Approximately 78.2 kDa

Greater than 95% as determined by Tris-Bis PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. Normally 8% trehalose is added as protectant before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.