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Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. Zusätzlich bieten wir Ihnen TGM3 Kits (21) und TGM3 Proteine (13) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 99 products:
Human Polyclonal TGM3 Primary Antibody für IF (p), IHC (p) - ABIN736253
Kawabe, Takano, Moriyama, Nakamura: Transglutaminases Derived from Astrocytes Accelerate Amyloid β Aggregation. in Neurochemical research 2017
Human Polyclonal TGM3 Primary Antibody für ELISA, WB - ABIN4362114
Yamane, Fukui, Sugimura, Itoh, Alea, Thomas, El Alaoui, Akiyama, Hitomi: Identification of a preferred substrate peptide for transglutaminase 3 and detection of in situ activity in skin and hair follicles. in The FEBS journal 2010
Human Polyclonal TGM3 Primary Antibody für IHC, IHC (p) - ABIN4362113
Uemura, Nakanishi, Kato, Saito, Nagino, Hirohashi, Kondo: Transglutaminase 3 as a prognostic biomarker in esophageal cancer revealed by proteomics. in International journal of cancer 2009
studies demonstrate that TGase (zeige F13A1 Antikörper)-catalyzed transamidation and activation of rac1 and cdc42 (zeige CDC42 Antikörper) results from stimulation of multiple types of receptors and this novel signaling pathway can regulate dendritic spine morphology and plasticity.
The two enzymes PADI3 (zeige PADI3 Antikörper) and TGM3, responsible for posttranslational protein modifications, and their target structural protein TCHH (zeige TCHH Antikörper) are all involved in hair shaft formation.
Data indicate a decrease in transglutaminases TG1 and TG3 transcripts by about 70% in foreskins from patients with balanitis xerotica obliterans (BXO) BXO in comparison with patients without BXO and an increase in transglutaminase TG2 (zeige TGM2 Antikörper) mRNA levels by 2.9 fold.
Our data collectively demonstrate that TGM3 can be a candidate tumor suppressor that is able to induce esophageal cancer cell proliferation and migration
mRNA expression of transglutaminase 1 (zeige TGM1 Antikörper) 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 (zeige RGS22 Antikörper)(rs7006527).
IgA (zeige IgA Antikörper)-anti-TG1 antibodies were found in 2% and IgA (zeige IgA Antikörper)-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 (zeige IgA Antikörper)-anti-TG1 and IgA (zeige IgA Antikörper)-anti-TG2 (zeige TGM2 Antikörper) 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.
study concludes that the classic wellhaarig mutations result from defects in Tgm3
The first signs of alopecia in mice of the +/Fgf5 (zeige FGF5 Antikörper)(go-Y) we/wewal/wal genotype appear only three days later than in double +/+ we/wewal/wal homozygotes.
Fluctuations of BMP2 (zeige BMP2 Antikörper) signaling pathway during hair cycles in skin with mutant genes we, wal and Fgf5 (zeige FGF5 Antikörper)(go).
Interaction of mutant genes Fgf5 (zeige FGF5 Antikörper)(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.
new information on the specific distribution of TGase 3
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