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mouse anti-Transglutaminase-2 (TG2) monoclonal antibody (7D2) 4432


Antibody summary

  • Mouse monoclonal to Transglutaminase-2 (TG2)
  • Suitable for: WB,ICC
  • Isotype: IgG3
  • 100 µg
SKU: 4432parent Category: Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in







1 mg/mL




Transglutaminase-2 (TG2)

available sizes

100 µg

Available product – mouse anti-Transglutaminase-2 (TG2) monoclonal antibody (7D2) 4432

Tested applications
Recommended dilutions
Immunoblotting: use at 1-5ug/mL. A band of ~80kDa is detected.

Immunocytochemistry: use at 2- 10ug/mL.

These are recommended concentrations.

Enduser should determine optimal concentrations for their applications.
Purified TG2 from guinea pig liver (accession no. P21980).
Size and concentration
100µg and
Storage Instructions
This product is stable for at least one (1) year at -20°C to -70°C. Reconstituted product should be stored in appropriate aliquots to avoid repeated freeze-thaw cycles.
Storage buffer
Lyophilized, 0.1M Tris, 0.1M glycine, 2% sucrose
protein affinty purification
Compatible secondaries
goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 5486
goat anti-mouse IgG, H&L chain specific, biotin conjugated, Conjugate polyclonal antibody 2685
goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody 7854
goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1706
goat anti-mouse IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1716
goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1721
Isotype control
Mouse monocolonal IgG3 - Isotype Control
target relevance
Protein names
Protein-glutamine gamma-glutamyltransferase 2 (EC (Erythrocyte transglutaminase) (Heart G alpha(h)) (hhG alpha(h)) (Isopeptidase TGM2) (EC 3.4.-.-) (Protein G alpha(h)) (G(h)) (Protein-glutamine deamidase TGM2) (EC (Protein-glutamine dopaminyltransferase TGM2) (EC 2.3.1.-) (Protein-glutamine histaminyltransferase TGM2)
Gene names
Protein family
Transglutaminase superfamily, Transglutaminase family
FUNCTION: Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (PubMed:9252372, PubMed:23941696, PubMed:31991788). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:7935379, PubMed:9252372, PubMed:27270573). Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:23941696, PubMed:24349085, PubMed:29618516, PubMed:30458214). Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca(2+) in response to various stresses (PubMed:7649299, PubMed:7592956, PubMed:18092889). When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (PubMed:12506096). Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components (PubMed:7935379, PubMed:9252372). In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (PubMed:23797785, PubMed:30867594). Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity). Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3 (PubMed:30867594, PubMed:32273471). Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (PubMed:30867594). Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (PubMed:32273471). Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (By similarity). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (PubMed:9623982, PubMed:20547769). Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (PubMed:9623982). May also act as an isopeptidase cleaving the previously formed cross-links (PubMed:26250429, PubMed:27131890). Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (PubMed:8943303). {ECO:0000250|UniProtKB:P08587, ECO:0000250|UniProtKB:P21981, ECO:0000269|PubMed:12506096, ECO:0000269|PubMed:1683874, ECO:0000269|PubMed:18092889, ECO:0000269|PubMed:20547769, ECO:0000269|PubMed:23797785, ECO:0000269|PubMed:23941696, ECO:0000269|PubMed:24349085, ECO:0000269|PubMed:26250429, ECO:0000269|PubMed:27131890, ECO:0000269|PubMed:29618516, ECO:0000269|PubMed:30458214, ECO:0000269|PubMed:30867594, ECO:0000269|PubMed:31991788, ECO:0000269|PubMed:32273471, ECO:0000269|PubMed:7592956, ECO:0000269|PubMed:7649299, ECO:0000269|PubMed:7935379, ECO:0000269|PubMed:8943303, ECO:0000269|PubMed:9252372, ECO:0000269|PubMed:9623982, ECO:0000303|PubMed:27270573}.; FUNCTION: [Isoform 2]: Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity. {ECO:0000269|PubMed:17116873}.
Catalytic activity
CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=; Evidence={ECO:0000255|PROSITE-ProRule:PRU10024, ECO:0000269|PubMed:23941696, ECO:0000269|PubMed:24349085, ECO:0000269|PubMed:31991788}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54817; Evidence={ECO:0000269|PubMed:23941696, ECO:0000269|PubMed:24349085, ECO:0000269|PubMed:31991788}; CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + serotonin = 5-serotonyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66552, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17052, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:167174, ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:30867594}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66553; Evidence={ECO:0000269|PubMed:30867594}; CATALYTIC ACTIVITY: Reaction=dopamine + L-glutaminyl-[protein] = 5-dopaminyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66556, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17053, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:59905, ChEBI:CHEBI:167175; Evidence={ECO:0000269|PubMed:32273471}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557; Evidence={ECO:0000269|PubMed:32273471}; CATALYTIC ACTIVITY: Reaction=histamine + L-glutaminyl-[protein] = 5-histaminyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66564, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17056, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:58432, ChEBI:CHEBI:167179; Evidence={ECO:0000269|PubMed:23797785}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565; Evidence={ECO:0000269|PubMed:23797785}; CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline + L-glutaminyl-[protein] = 5-(R)-noradrenalinyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66560, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17054, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011, ChEBI:CHEBI:72587, ChEBI:CHEBI:167178; Evidence={ECO:0000250|UniProtKB:P08587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561; Evidence={ECO:0000250|UniProtKB:P08587}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=; Evidence={ECO:0000269|PubMed:20547769, ECO:0000269|PubMed:9623982}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442; Evidence={ECO:0000269|PubMed:20547769, ECO:0000269|PubMed:9623982};
Subellular location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24349085, ECO:0000269|PubMed:29618516, ECO:0000269|PubMed:9575137}. Nucleus {ECO:0000269|PubMed:29618516, ECO:0000269|PubMed:9575137}. Chromosome {ECO:0000269|PubMed:9575137}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12506096, ECO:0000269|PubMed:1683874}. Cell membrane {ECO:0000250|UniProtKB:Q9WVJ6}. Mitochondrion {ECO:0000269|PubMed:24349085}. Note=Mainly localizes to the cytosol (PubMed:9575137). Present at much lower level in the nucleus and chromatin (PubMed:9575137). Also secreted via a non-classical secretion pathway to the extracellular matrix (PubMed:27270573). {ECO:0000269|PubMed:9575137, ECO:0000303|PubMed:27270573}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17116873}.
SUBUNIT: Monomer (PubMed:25192068). Interacts with phospholipase C; promoting alpha-1 adrenergic receptor signaling (PubMed:7592956). Interacts with PLCD1 (By similarity). {ECO:0000250|UniProtKB:Q9WVJ6, ECO:0000269|PubMed:25192068, ECO:0000269|PubMed:7592956}.; SUBUNIT: [Isoform 2]: Homooligomer. {ECO:0000269|PubMed:17116873}.
Post-translational modification
PTM: Disulfide bond formation inactivates the calcium-dependent acyltransferase activity (PubMed:20547769). Cys-370 can form disulfide bonds with both Cys-230 and Cys-371: formation of a disulfide bond between Cys-230 and Cys-370 facilitates formation of the disulfide between Cys-370 and Cys-371, which promotes inactivation of the acyltransferase activity (PubMed:20547769). May also form interchain disulfids between Cys-230 and Cys-370 (PubMed:25192068). Ca(2+) protects against disulfide bond formation and inactivation (PubMed:20547769). {ECO:0000269|PubMed:20547769, ECO:0000269|PubMed:25192068}.; PTM: Auto-transglutaminated: Forms covalent cross-links mediated by transglutaminase between Gln-633 and the epsilon-amino group of a lysine residue of itself or HMGB1, forming homopolymers and heteropolymers, respectively. {ECO:0000250|UniProtKB:P08587}.; PTM: S-nitrosylated, leading to inactivation of the acyltransferase activity. {ECO:0000250|UniProtKB:P21981}.
Target Relevance information above includes information from UniProt accession : P21980
The UniProt Consortium


Immunoblotting: use at 1-5ug/ml. A band of ~80kDa is detected. Detection of TG2 in human erythroctyes with #4432.


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



relevant to this product
Western blot


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