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Human Dolichol-Linked Oligosaccharide Biosynthetic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: GFAT1, glutamine:fructose-6-phosphate aminotransferase 1, is the rate-limiting enzyme of the hexosamine biosynthesis pathway (1). This enzyme catalyzes the conversion of fructose-6-phosphate and glutamine to glucosamine-6-phosphate and glutamate (2). The hexosamine biosynthesis pathway generates the building blocks for protein and lipid glycosylation (2). Furthermore, studies suggest that increased activity of this pathway is a contributing factor to hyperglycemia-induced insulin resistance (1,2). GFAT1 is more active in non-insulin-dependent diabetes mellitus (NIDDM) patients (3). Transgenice mice overexpressing this enzyme in skeletal muscle and adipose tissue show an insulin resistance phenotype (4,5). GFAT2, an isoenzyme of GFAT1, was later identified (6, 7). Studies show that the regulation of GFAT2 is different from that of GFAT1, suggesting differential regulation of the hexosamine pathway in different tissues (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: GFAT1, glutamine:fructose-6-phosphate aminotransferase 1, is the rate-limiting enzyme of the hexosamine biosynthesis pathway (1). This enzyme catalyzes the conversion of fructose-6-phosphate and glutamine to glucosamine-6-phosphate and glutamate (2). The hexosamine biosynthesis pathway generates the building blocks for protein and lipid glycosylation (2). Furthermore, studies suggest that increased activity of this pathway is a contributing factor to hyperglycemia-induced insulin resistance (1,2). GFAT1 is more active in non-insulin-dependent diabetes mellitus (NIDDM) patients (3). Transgenice mice overexpressing this enzyme in skeletal muscle and adipose tissue show an insulin resistance phenotype (4,5). GFAT2, an isoenzyme of GFAT1, was later identified (6, 7). Studies show that the regulation of GFAT2 is different from that of GFAT1, suggesting differential regulation of the hexosamine pathway in different tissues (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GFAT1, glutamine:fructose-6-phosphate aminotransferase 1, is the rate-limiting enzyme of the hexosamine biosynthesis pathway (1). This enzyme catalyzes the conversion of fructose-6-phosphate and glutamine to glucosamine-6-phosphate and glutamate (2). The hexosamine biosynthesis pathway generates the building blocks for protein and lipid glycosylation (2). Furthermore, studies suggest that increased activity of this pathway is a contributing factor to hyperglycemia-induced insulin resistance (1,2). GFAT1 is more active in non-insulin-dependent diabetes mellitus (NIDDM) patients (3). Transgenice mice overexpressing this enzyme in skeletal muscle and adipose tissue show an insulin resistance phenotype (4,5). GFAT2, an isoenzyme of GFAT1, was later identified (6, 7). Studies show that the regulation of GFAT2 is different from that of GFAT1, suggesting differential regulation of the hexosamine pathway in different tissues (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: β-galactosidase (also known as β-gal) is an essential hydrolase enzyme that catalyzes the hydrolysis of galactose-containing carbohydrates into monosaccharides. Substrates of β-galactosides include lactose, various glycoproteins, ganglioside GM1, and lactosylceramides. β-galactosidase is used widely in molecular biology; for example, isolation of recombinant bacteria during molecular cloning utilizes α-complementation of the bacterial β-galactosidase gene (lacZ) in the presence of a β-gal substrate to identify recombinant clones (1). In cell biology, Senescence-Associated beta-galactosidase (SA-β-gal), defined as β-gal activity at pH 6.0, is a widely used marker of replicative senescence. While initially thought to derive from a unique isoform of β-galactosidase expressed specifically in senescent cells (2), SA-β-gal activity was subsequently shown to result from overexpression and accumulation of β-galactosidase in endogenous lysosomes, and is not specifically required for replicative senescence (3).