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|Recombinant Human GFAT protein (Catalog#11071-HNAE)|
|0.2 μm filtered solution in PBS with 5% trehalose|
|Produced in rabbits immunized with purified, recombinant Human GFAT (rh GFAT; Catalog#11071-HNAE; AAA58502.1; Gln 332-Glu 699). GFAT specific IgG was purified by human GFAT affinity chromatography .|
|Human GFAT / GFPT1|
ELISA: 0.1-0.2 μg/mL
This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect Human GFAT. The detection limit for Human GFAT is approximately 0.00975 ng/well.
|This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free.|
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Glutamine:fructose-6-phosphate amidotransferase 1 (GFAT), also known as GFPT1, is a member of the N-terminal nucleophile aminotransferases and the first rate-limiting enzyme for the entry of glucose into the hexosamine biosynthesis pathway (HBP) in mammals. GFAT transfers the amino group from the L-glutamine amide to the D-fructose 6-phosphate, producing glutamic acid and glucosamine 6-phosphate. GFAT exists as a homotetramer in cytoplasm, and is proposed to be most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. The full length of human GFAT contains 1 glutamine amidotransferase type-2 domain which catalyzes amide nitrogen transfer from glutamine to the appropriate substrate, and 2 SIS (Sugar Isomerase) domains found in many phosphosugar isomerases and phosphosugar binding proteins.Two isoforms of gfat have been identified: GFAT1 is predominantly expressed in skeletal muscle, whereas GFAT2 is expressed mainly in the central nervous system.