AV47471
Anti-TGM2 (AB1) antibody produced in rabbit
affinity isolated antibody
Synonym(s):
Anti-TG2, Anti-TGC, Anti-Transglutaminase 2 (C polypeptide, protein-glutamine-γ-glutaMylTransferase)
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All Photos(2)
About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
62 kDa
species reactivity
rat, mouse, rabbit, human
concentration
0.5 mg - 1 mg/mL
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... TGM2(7052)
General description
TGM2 codes for a transglutaminase that catalyzes the crosslinking of protein via epsilon-gamma glutamyl lysine isopeptide bonds. Tgm2/Gh is known to play a role in the retinoic acid-induced transdifferentiation of mucosal epithelial cells. It functions as a biomarker for predicting treatment efficacy in laryngeal cancer patients undergoing radiotherapy. It is also associated with drug sensitivity in breast cancer.
Rabbit Anti-TGM2 antibody recognizes chicken, bovine, human, mouse, rat, and zebrafish TGM2.
Rabbit Anti-TGM2 antibody recognizes chicken, bovine, human, mouse, rat, and zebrafish TGM2.
Immunogen
Synthetic peptide directed towards the middle region of human TGM2
Application
Rabbit Anti-TGM2 antibody is suitable for western blot applications at a concentration of 0.25 μg/ml.
Biochem/physiol Actions
Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, TGM2 is the autoantigen implicated in celiac disease.Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene.Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene.
Sequence
Synthetic peptide located within the following region: VGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Lingbao Ai et al.
Carcinogenesis, 29(3), 510-518 (2008-01-05)
Tissue transglutaminase (TG2) is a ubiquitously expressed enzyme capable of catalyzing protein cross-links. TG2-dependent cross-links are important in extracellular matrix integrity and it has been proposed that this TG2 activity establishes a barrier to tumor spread. Furthermore, TG2 controls sensitivity
Akiko Obinata et al.
The International journal of developmental biology, 55(10-12), 933-943 (2012-01-19)
We previously demonstrated that retinoic acid (RA) induces epidermis to transdifferentiate to mucosal epithelium with goblet cells in chick embryonic cultured skin. To characterize the molecular mechanism of this transdifferentiation process, we used rat embryonic cultured skin and immunohistochemistry to
I Marafini et al.
Alimentary pharmacology & therapeutics, 40(8), 974-981 (2014-08-13)
The clinical presentation of organic and functional intestinal disorders can overlap and clinicians often rely on invasive and time-consuming procedures to make a final diagnosis. Regenerating islet-derived 3-alpha (Reg3α) is detectable in the circulation of patients with intestinal graft-versus host
Pasqualino De Antonellis et al.
Molecular & cellular proteomics : MCP, 13(8), 2114-2131 (2014-06-11)
Several genes encoding for proteins involved in proliferation, invasion, and apoptosis are known to be direct miR-34a targets. Here, we used proteomics to screen for targets of miR-34a in neuroblastoma (NBL), a childhood cancer that originates from precursor cells of
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