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Transglutaminase II (TGM2) (FN Binding Domain) Antibody [TGM2/3612]

Additional information

Catalog Number: 7052-MSM2
Reactivity:

, ,

Gene:

Host:

In Stock

Trial Size Available

Carrier-Free Available

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In Stock
Catalog Number Formulation Size Price
7052-MSM2-P0
Purified Ab with BSA and Azide at 200ug/ml
20ug
$259.00
7052-MSM2-P1
Purified Ab with BSA and Azide at 200ug/ml
100ug
$559.00
7052-MSM2-P1ABX
Purified Ab WITHOUT BSA and Azide at 1.0mg/ml
100ug
$559.00
Flat Rate Domestic: $95 | Orders outside the US - Contact Us for Order Information | Ships next business day
Transglutaminase II (TGM2) (FN Binding Domain) Antibody

Formalin-fixed, paraffin-embedded human placenta stained with Transglutaminase II Mouse Monoclonal Antibody (TGM2/3612). Inset: PBS instead of primary antibody; secondary only negative control.

Transglutaminase II (TGM2) (FN Binding Domain) Antibody - Image 2

SDS-PAGE Analysis of Purified Transglutaminase II Mouse Monoclonal Antibody (TGM2/3612). Confirmation of Purity and Integrity of Antibody.

  • Flow
  • IF
  • IHC
  • Documents
  • Applications & Dilutions
  • Product Properties
  • other information

Documents

Document Name
Datasheet Download Here
Material Safety Data Sheet Download Here

Applications & Dilutions

Applications Tested Dilutions Protocol Note
Flow Cytometry (Flow) 1-2ug/million cells Flow Cytometry Protocol
Immunofluorescence (IF) 1-3ug/ml
Immunohistochemistry (IHC) 1-2ug/ml IHC Protocol 30 min at RT. Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95°C followed by cooling at RT for 20 minutes

Product Properties

Antibody Type
Mouse Monoclonals
Host
Mouse
Applications
Flow Cytometry, Immunofluorescence, Immunohistochemistry
Species Reactivity
Human, Mouse, Rat
Clone
TGM2/3612
Isotype
IgG1
Light Chain
Kappa
Cellular Localization
Cell membrane, Chromosome, Cytoplasm, Cytosol, Extracellular matrix, Extracellular space, Mitochondrion, Nucleus, Perinuclear region, Secreted
Gene Name
TGM2
Positive Control
Brain, HUVEC cells.Endothelial cells in placenta, Liver, or breast carcinoma. Smooth muscle cells of any origin.
Immunogen
Recombinant full-length human TGM2 protein
Storage & Stability
Antibody with azide - store at 2 to 8 °C. Antibody without azide - store at -20 to -80 °C. Antibody is stable for 24 months. Non-hazardous. No MSDS required.
Supplied as
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
Limitations
This antibody is available for research use only and is not approved for use in diagnosis.

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Other Information

Functions
  • 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).
  • Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity.
Key References
  • Yamanishi, K., et al. 1991. Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture. Biochem. Biophys. Res. Commun. 175: 906-913.
PubMed Links
Warranty
There are no warranties, expressed or implied, which extend beyond this description. Company is not liable for any personal injury or economic loss resulting from this product.
Entrez Gene ID
7052
SwissProt
P21980
Chromosome Location
20q12
Mol. Weight of Antigen
77-85kDa
Alternate 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, Protein-glutamine gamma-glutamyltransferase 2; TG2; TGase C; TGase H; TGase-2; TgaseII; TGC; TGM2; Tissue type transglutaminase; Transglutaminase 2 C polypeptide; Transglutaminase H; tTG; tTGas

Summary

Tissue transglutaminase (tTG) is a 75 kDa monomeric globular protein expressed in the majority of cells and tissues. tTG localizes mainly in the cytoplasm but some tGT is present on the cell surface and is association with the extracellular matrix. In addition to its guanosine triphosphatase (GTPase) activity, tTG catalyzes the posttranslational modification of proteins by transamidation of available glutamine residues (Monsonego, 1997). Extracellular tTG is able to bind to and cross-link several ECM proteins and may function to stabilize the ECM and basement membranes. The protein is translated as a fully active enzyme and there is no evidence for proteolytic activation.High constitutive expression and accumulation of active tTG is observed in (among others) endothelial cells, platelets, vascular smooth muscle cells and epithelial cells of the lens. tTG is expressed at very low levels in skeletal muscle cells and neurons and may be difficult to detect in these cell/tissue types.

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