Recombinant Human Transglutaminase 2 protein (His tag) is a Human Full Length protein, in the 1 to 687 aa range, expressed in Baculovirus infected insect, with >97% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Key facts
- Purity
- >97% SDS-PAGE
- Endotoxin level
- < 1 EU/µg
- Expression system
- Baculovirus infected insect cells
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M A E E L V L E R C D L E L E T N G R D H H T A D L C R E K L V V R R G Q P F W L T L H F E G R N Y E A S V D S L T F S V V T G P A P S Q E A G T K A R F P L R D A V E E G D W T A T V V D Q Q D C T L S L Q L T T P A N A P I G L Y R L S L E A S T G Y Q G S S F V L G H F I L L F N A W C P A D A V Y L D S E E E R Q E Y V L T Q Q G F I Y Q G S A K F I K N I P W N F G Q F E D G I L D I C L I L L D V N P K F L K N A G R D C S R R S S P V Y V G R V V S G M V N C N D D Q G V L L G R W D N N Y G D G V S P M S W I G S V D I L R R W K N H G C Q R V K Y G Q C W V F A A V A C T V L R C L G I P T R V V T N Y N S A H D Q N S N L L I E Y F R N E F G E I Q G D K S E M I W N F H C W V E S W M T R P D L Q P G Y E G W Q A L D P T P Q E K S E G T Y C C G P V P V R A I K E G D L S T K Y D A P F V F A E V N A D V V D W I Q Q D D G S V H K S I N R S L I V G L K I S T K S V G R D E R E D I T H T Y K Y P E G S S E E R E A F T R A N H L N K L A E K E E T G M A M R I R V G Q S M N M G S D F D V F A H I T N N T A E E Y V C R L L L C A R T V S Y N G I L G P E C G T K Y L L N L N L E P F S E K S V P L C I L Y E K Y R D C L T E S N L I K V R A L L V E P V I N S Y L L A E R D L Y L E N P E I K I R I L G E P K Q K R K L V A E V S L Q N P L P V A L E G C T F T V E G A G L T E E Q K T V E I P D P V E A G E E V K V R M D L L P L H M G L H K L V V N F E S D K L K A V K G F R N V I I G P A
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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:23941696, PubMed:31991788, PubMed:9252372). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:27270573, PubMed:28198360, PubMed:7935379, PubMed:9252372). 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:18092889, PubMed:7592956, PubMed:7649299). 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:20547769, PubMed:9623982). 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). Isoform 2. Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity.
Alternative names
Protein-glutamine gamma-glutamyltransferase 2, Erythrocyte transglutaminase, Heart G alpha(h), Isopeptidase TGM2, Protein G alpha(h), Protein-glutamine deamidase TGM2, Protein-glutamine dopaminyltransferase TGM2, Protein-glutamine histaminyltransferase TGM2, Protein-glutamine noradrenalinyltransferase TGM2, Protein-glutamine serotonyltransferase TGM2, Tissue transglutaminase, Transglutaminase C, Transglutaminase H, Transglutaminase II, Transglutaminase-2, hhG alpha(h), G(h), tTG, tTgase, TG(C), TGC, TGase C, TGase H, TGase II, TG2, TGase-2, hTG2, TGM2
Recommended products
Recombinant Human Transglutaminase 2 protein (His tag) is a Human Full Length protein, in the 1 to 687 aa range, expressed in Baculovirus infected insect, with >97% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
Key facts
- Purity
- >97% SDS-PAGE
- Endotoxin level
- < 1 EU/µg
- Expression system
- Baculovirus infected insect cells
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- P21980-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.61% Tris, 0.58% Sodium chloride, 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Sequence info
Amino acid sequence
- M A E E L V L E R C D L E L E T N G R D H H T A D L C R E K L V V R R G Q P F W L T L H F E G R N Y E A S V D S L T F S V V T G P A P S Q E A G T K A R F P L R D A V E E G D W T A T V V D Q Q D C T L S L Q L T T P A N A P I G L Y R L S L E A S T G Y Q G S S F V L G H F I L L F N A W C P A D A V Y L D S E E E R Q E Y V L T Q Q G F I Y Q G S A K F I K N I P W N F G Q F E D G I L D I C L I L L D V N P K F L K N A G R D C S R R S S P V Y V G R V V S G M V N C N D D Q G V L L G R W D N N Y G D G V S P M S W I G S V D I L R R W K N H G C Q R V K Y G Q C W V F A A V A C T V L R C L G I P T R V V T N Y N S A H D Q N S N L L I E Y F R N E F G E I Q G D K S E M I W N F H C W V E S W M T R P D L Q P G Y E G W Q A L D P T P Q E K S E G T Y C C G P V P V R A I K E G D L S T K Y D A P F V F A E V N A D V V D W I Q Q D D G S V H K S I N R S L I V G L K I S T K S V G R D E R E D I T H T Y K Y P E G S S E E R E A F T R A N H L N K L A E K E E T G M A M R I R V G Q S M N M G S D F D V F A H I T N N T A E E Y V C R L L L C A R T V S Y N G I L G P E C G T K Y L L N L N L E P F S E K S V P L C I L Y E K Y R D C L T E S N L I K V R A L L V E P V I N S Y L L A E R D L Y L E N P E I K I R I L G E P K Q K R K L V A E V S L Q N P L P V A L E G C T F T V E G A G L T E E Q K T V E I P D P V E A G E E V K V R M D L L P L H M G L H K L V V N F E S D K L K A V K G F R N V I I G P A
- Accession
- P21980
- Protein length
- Full Length
- Predicted molecular weight
- 79.6 kDa
- Amino acids
- 1 to 687
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Lyophilized
- Additional notes
The protein is affinity purified.
General info
- 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:23941696, PubMed:31991788, PubMed:9252372). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:27270573, PubMed:28198360, PubMed:7935379, PubMed:9252372). 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:18092889, PubMed:7592956, PubMed:7649299). 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:20547769, PubMed:9623982). 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).
- Sequence similarities
Belongs to the transglutaminase superfamily. Transglutaminase family.
- Post-translational modifications
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).
- Subcellular localisation
- Nucleus, Mitochondrion
Storage
- Shipped at conditions
- Ambient - Can Ship with Ice
- Appropriate short-term storage conditions
- -20°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Transglutaminase 2 also known as TG2 or tissue transglutaminase is an enzyme with a mass of approximately 74 kDa. It catalyzes the formation of covalent bonds by crosslinking glutamine residues and lysine residues in proteins. This enzyme is widely expressed in various tissues including the liver heart and lungs. It can act as a GTPase a kinase and a protein disulfide isomerase highlighting its multifunctional nature. Additionally transglutaminase 2 associates with cell membranes cytoskeleton and extracellular matrix indicating its versatile involvement in cellular processes.
- Biological function summary
Transglutaminase 2 plays roles in cell adhesion wound healing and the immune response. It mediates extracellular matrix stabilization through crosslinking structural proteins which is critical for tissue repair. The enzyme does not typically form a stable part of a large complex but interacts with fibronectin as a binding partner highlighting its role in cellular adhesion and migration. The enzymatic activity of transglutaminase 2 helps maintain tissue integrity by modifying extracellular and intracellular proteins.
- Pathways
Transglutaminase 2 contributes significantly to the integrin-mediated signaling pathway and the apoptosis pathway. It assists in the modulation of cell-matrix interactions by crosslinking matrix proteins which is important for integrin signaling. During apoptosis transglutaminase 2 promotes cellular processes that lead to cell death via its involvement in nuclear condensation and DNA fragmentation. In these pathways proteins such as fibronectin and integrins interact with transglutaminase 2 facilitating its regulatory functions.
- Associated diseases and disorders
Transglutaminase 2 is associated with celiac disease and neurodegenerative disorders like Huntington's disease. Its autoantigenic properties make it a target in celiac disease where antibodies against transglutaminase 2 play a role in the pathology by affecting intestinal tissue. In Huntington's disease transglutaminase 2 contributes to the formation of protein aggregates which are toxic to neurons. This enzyme's interactions with proteins such as gliadin in celiac disease and huntingtin in Huntington's disease are central to its pathogenic mechanism.
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SDS-PAGE - Recombinant Human Transglutaminase 2 protein (His tag) (ab276359)
SDS-PAGE analysis of ab276359
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