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Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. Additionally we are shipping TGM3 Kits (14) and TGM3 Proteins (13) and many more products for this protein.
Showing 10 out of 90 products:
Human Polyclonal TGM3 Primary Antibody for WB - ABIN2777149
Zocchi, Terrinoni, Candi, Ahvazi, Bagetta, Corasaniti, Lena, Melino: Identification of transglutaminase 3 splicing isoforms. in The Journal of investigative dermatology 2007
Human Polyclonal TGM3 Primary Antibody for EIA, IHC (fro) - ABIN191748
Sárdy, Kárpáti, Merkl, Paulsson, Smyth: Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis. in The Journal of experimental medicine 2002
mRNA expression of transglutaminase 1 (show TGM1 Antibodies) and transglutaminase 3 was significantly decreased in patients with chronic periodontitis compared with a healthy control group.
Transglutaminase 3 present in the IgA aggregates in dermatitis herpetiformis skin is enzymatically active and binds soluble fibrinogen.
New basal cell carcinoma susceptibility loci were identified at TGM3 (rs214782) and RGS22 (show RGS22 Antibodies)(rs7006527).
IgA-anti-TG1 antibodies were found in 2% and IgA-anti-TG3 antibodies in 3% of patients with active atopic dermatitis (AD). Two out of the 5 patients with AD and concomitant celiac disease had IgA-anti-TG1 and IgA-anti-TG2 (show TGM2 Antibodies) antibodies.
TGM3, a candidate tumor suppressor, contributes to the carcinogenesis and development of human head and neck cancer.
Genetic variation in the epidermal transglutaminase genes is not associated with atopic dermatitis.
The low expression of TGM3 may contribute to the carcinogenesis and development of laryngeal carcinoma.
TGM3 in immunoglobulin A (IgA) and TGM3 immune complexes is responsible for cross-linking and tight binding of IgA to connective tissue in the dermis and explains the IgA deposits in dermatitis herpetiformis skin long after signs of disease are resolved.
findings lend credence to the notion that TG3 and TG6 are involved in the gluten-induced autoimmune responses of dermatitis herpetiformis and gluten ataxia (show USP14 Antibodies)
new information on the specific distribution of TGase 3
study concludes that the classic wellhaarig mutations result from defects in Tgm3
The first signs of alopecia in mice of the +/Fgf5 (show FGF5 Antibodies)(go-Y) we/wewal/wal genotype appear only three days later than in double +/+ we/wewal/wal homozygotes.
Fluctuations of BMP2 (show BMP2 Antibodies) signaling pathway during hair cycles in skin with mutant genes we, wal and Fgf5 (show FGF5 Antibodies)(go).
Interaction of mutant genes Fgf5 (show FGF5 Antibodies)(go-Y), we, and wal changes the duration of hair growth cycles in mice
The clinically uninvolved skin in TGM3 knockout mice showed impaired barrier function and higher susceptibility to FITC sensitization indicating that TGM3 has a significant contribution to the functionally intact cutaneous barrier.
Loss of Tgm3 is associated with defective hair development.
The expression of TGM3 may play a important role in the epidermis differentiation in embryogenesis.
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 consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle.
E polypeptide, protein-glutamine-gamma-glutamyltransferase
, TGase E
, protein-glutamine gamma-glutamyltransferase E
, transglutaminase E
, E polypeptide
, TG E