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|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant human protein purified from E.coli.|
|Purification||Ammonium sulfate precipitation|
|Storage buffer||HEPES with 0.15M NaCl, 0.01% BSA, 50% glycerol|
|Contains||0.03% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunoprecipitation (IP)||1 µl|
|Western Blot (WB)||1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
A suggested positive control for this product is U87-MG cells.
Transglutaminase (TGase) catalyses the crosslink of proteins by forming e-(g-glutamyl) lysine isopeptide bonds and requires the binding of Ca2+ for its activity. In mammals, eight distinct TGase isoenzymes have been identified. Tissue transglutaminase (tTGase), also known as TGase 2, has four distinct domains: N-terminal b-sandwich, catalytic core and two C-terminal b-barrel domains. tTGase may have a role in cell death, cell proliferation, cell differentiation, and receptor-mediated endocytosis. In the Alzheimer's disease brain, the elevated tTGase activity is manifested by polymerization of a number of proteins, including Ab peptide, b-amyloid precursor protein and the tau protein, with formation of neurofibrillary tangles.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
C polypeptide; C polypeptide, protein-glutamine-gamma-glutamyltransferase; G alpha h; G protein alpha subunit Gh class; TGase C; TGase H; TGase-2; tissue transglutaminase; transglutaminase C; transglutaminase H; transglutaminase-2
TG(C); TGC; TGM2