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Aspartylglucosaminidase is involved in the catabolism of N-linked oligosaccharides of glycoproteins. Additionally we are shipping AGA Antibodies (24) and AGA Proteins (13) and many more products for this protein.
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We show that gene-silenced cells show specifically reduced AGA activity and store globotriaosylceramide. In gene-silenced cells, release of the neurotransmitter acetylcholine is significantly reduced, demonstrating that this model may be used to study specific neuronal functions such as neurotransmitter release in Fabry disease
study reports 2 novel aspartylglucosaminidase gene mutations, one in Qatari twins with an early, perinatal presentation not previously described for aspartylglucosaminuria and the other in 3 Turkish children with newly diagnosed aspartylglucosaminuria and a more classical disease course
[review] Natural killer (NK) cell tumors, subtypes of myeloid leukemias and T-cell lymphomas respond to ASNase; ovarian carcinomas and other solid tumors have been proposed as additional targets for ASNase, with a potential role for glutaminase (show GLS ELISA Kits). activity.
Molecular mechanism for the autoproteolytic activation of aspartylglucosaminidase.
A new point mutation, c.44T>G, found in a Finnish compound heterozygote causes a L15R AA substitution in the signal sequence of the AGA enzyme, affecting AGA translocation by altering a critical hydrophobic core structure in the signal sequence.
aspartylglucosaminidase may have a role in development of congenital disorders of glycosylation type I
The amino acid substitutions in aspartylglucosaminidase responsible for aspartylglucosaminuria were classified and divided in three groups.
Increased AGA plasma activity, although a consistent finding in congenital disorders of glycosylation patients, is not specific to this group of disorders.
Aspartylglucosaminidase is involved in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves asparagine from N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins. The lysosomal storage disease aspartylglycosaminuria is caused by a deficiency in the AGA enzyme. Alternatively spliced transcript variants have been identified.
, N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
, aspartylglucosylamine deaspartylase