Human TGM3 / Transglutaminase 3 Protein (His Tag)

TGE

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Catalog Number	P11923-H07B
Organism Species	Human
Host	Baculovirus-Insect Cells
Synonyms	TGE
Molecular Weight	The recombinant human TGM3 consists of 710 amino acids and predicts a molecular mass of 78.8 kDa. It migrates as an approximately 70 kDa band in SDS-PAGE under reducing conditions.
predicted N	His
SDS-PAGE
Purity	> 95 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human TGM3 (Q08188) (Ala 2-Glu 693) was expressed, with a polyhistidine tag at the N-terminus.
Bio-activity	Measured by its ability to cleave a synthetic peptide Benzyloxycarbonyl-Gln-Gly and NH2OH. The specific activity is > 450 pmoles/min/μg.
Research Area	Immunology |Signal Transduction |Metabolism |Amino Acids
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.5, 10% gly 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	Transglutaminases (TGase) are a family of calcium-dependent acyl-transfer enzymes ubiquitously expressed in mammalian cells and responsible for catalyzing covalent cross-links between proteins or peptides. Transglutaminase 3 (TGM3) is a member of a family of Ca2+-dependent enzymes that catalyze covalent cross-linking reactions between proteins or peptides. TGM3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. Calcium-activated TGM3 can bind, hydrolyze, and is inhibited by GTP, despite lacking structural homology with other GTP binding proteins. TGM3 displays a diffuse cytoplasmic distribution in vitro consistent with its proposed role in the early phase of cornified cell envelope assembly in the cytoplasm. TGM3-driven specific isopeptide bonds between intermediate filaments and KAPs participate to the progressive scaffolding of the hair shaft. Additionally, TGM3 may be a novel prognostic biomarker for esophageal squamous cell carcinoma (ESCC).
Reference	Ahvazi B, et al. (2002) Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation. EMBO J. 21(9): 2055-67. Hitomi K, et al. (2003) Analysis of epidermal-type transglutaminase (transglutaminase 3) in human stratified epithelia and cultured keratinocytes using monoclonal antibodies. J Dermatol Sci. 32(2): 95-103. Ahvazi B, et al. (2004) The emerging structural understanding of transglutaminase 3. J Struct Biol. 147(2): 200-7. Ahvazi B, et al. (2004) Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium. J Biol Chem. 279(8): 7180-92. Uemura N, et al. (2009) Transglutaminase 3 as a prognostic biomarker in esophageal cancer revealed by proteomics. Int J Cancer. 124(9): 2106-15. Thibaut S, et al. (2009) Transglutaminase-3 enzyme: a putative actor in human hair shaft scaffolding? J Invest Dermatol. 129(2): 449-59.