protein

Tissue Transglutaminase, Recombinant, Human

MBS6120599

0.1 mg

390 USD

Recombinant Protein

Tissue Transglutaminase, Recombinant, Human

Tissue Transglutaminase

tissue transglutaminase; Protein-glutamine gamma-glutamyltransferase 2; protein-glutamine gamma-glutamyltransferase 2; TG(C); TGase C; TGase H; TGase-2; TGase-H; transglutaminase C; transglutaminase H; transglutaminase-2; tissue transglutaminase; protein-glutamine-gamma-glutamyltransferase; C polypeptide, protein-glutamine-gamma-glutamyltransferase; transglutaminase 2; Tissue transglutaminase; Transglutaminase C; TG(C); TGC; TGase C; Transglutaminase H; TGase H; Transglutaminase-2

TGM2; TGM2; TG2; TGC; GNAH; G-ALPHA-h; TG(C); TGC; TGase C; TGase H; TGase-2

TGM2_HUMAN

>95% (SDS-PAGE)

Supplied as a lyophilized powder from 50mM Tris-HCl, pH 7.5, 1mM EDTA, 1mM HABA, 1mM PMSF.

~1mg/ml (after reconstitution)

Lyophilized powder may be stored at -20 degree C. Stable for 12 months after receipt. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

ELISA (EL/EIA)

Suitable for ELISA. Optimal dilutions to be determined by the researcher.

Reconstitution: Reconstitute with 100ul sterile ddH2O.

Molecular Biology; MB-Enzymes

Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig. Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site aa eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins. Recombinant protein corresponding to the N-terminal region of human Tissue Transglutaminase, expressed in HEK 293-EBNA cell line, fused to His-Tag.

13183616

AAK15272.1

P21980

77,329 Da

Huntington's Disease Pathway (83100); Huntington's Disease Pathway (512); Thromboxane A2 Receptor Signaling Pathway (138060)

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. [provided by RefSeq, Jul 2008]

TGM2: an enzyme of the transglutaminase family that catalyzes the crosslinking of proteins and the conjugation of polyamines to proteins. 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. Is the autoantigen in coeliac disease and plays a role in apoptosis, cellular differentiation and matrix stabilisation. Three alternatively spliced isoforms have been described. Protein type: Transferase; EC 2.3.2.13. Chromosomal Location of Human Ortholog: 20q12. Cellular Component: focal adhesion; mitochondrion; plasma membrane; cytosol. Molecular Function: protein domain specific binding; protein binding; GTP binding; protein-glutamine gamma-glutamyltransferase activity; metal ion binding. Biological Process: elevation of cytosolic calcium ion concentration during G-protein signaling, coupled to IP3 second messenger (phospholipase C activating); positive regulation of cell adhesion; positive regulation of I-kappaB kinase/NF-kappaB cascade; isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; positive regulation of apoptosis; positive regulation of smooth muscle cell proliferation; reduction of endoplasmic reticulum calcium ion concentration; blood vessel remodeling; protein homooligomerization; apoptotic cell clearance; elevation of mitochondrial calcium ion concentration; positive regulation of inflammatory response

0.1 mg

390 USD