AV47472
Anti-TGM2 (AB2) antibody produced in rabbit
affinity isolated antibody
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Synonym(s):
Anti-TG2, Anti-TGC, Anti-Transglutaminase 2 (C polypeptide, protein-glutamine-γ-glutaMylTransferase)
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
77 kDa
species reactivity
human
concentration
0.5 mg - 1 mg/mL
technique(s)
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 human, mouse, rat, and bovineTGM2.
Rabbit Anti-TGM2 antibody recognizes human, mouse, rat, and bovineTGM2.
Immunogen
Synthetic peptide directed towards the N terminal region of human TGM2
Application
Rabbit Anti-TGM2 antibody is suitable for western blot applications at a concentration of 0.5 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.
Sequence
Synthetic peptide located within the following region: MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNY
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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
Ting Jin et al.
Journal of translational medicine, 10, 64-64 (2012-03-31)
This study was designed to determine the pattern and correlation between expression of the HIF-1α transcriptional targets TGM2 and BNIP3 in laryngeal cancer, and investigate the association of BNIP3 and TGM2 with clinical outcome in laryngeal squamous cell carcinoma (SCC)
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
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