Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Rat (Rattus) Anticorps:
anti-Mouse (Murine) Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Human Monoclonal AGLU Primary Antibody pour WB - ABIN920552
Hilkens, Tager, Buijs, Brouwer-Kelder, Van Thienen, Tegelaers, Hilgers: Monoclonal antibodies against human acid alpha-glucosidase. dans Biochimica et biophysica acta 1982
Mechanistic Pathway on Human alpha-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations
MGAM, or nearby regulatory elements, may be involved in the etiology of oral clefts.
Starch internal structure modulates its susceptibility to MGAM. The internal branch amounts negatively affect the glucose release rate.
The over-expression of MGAM was confirmed with a 6.6 fold increase in expression at the mRNA level whereas the fold change in ADAM9 demonstrated a 1.6 fold increase.
Findings suggest that C-terminal subunits of recombinant maltase-glucoamylase (MGAM) assists alpha-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies.
These results suggest that the N-terminal and C-terminal catalytic domains of maltase-glucoamylase differ in their substrate specificities and inhibitor tolerance despite their structural relationship
we report crystal structures of C-terminal maltase-glucoamylase alone at a resolution of 3.1 angstroms, and in complex with its inhibitor acarbose
analysis of substrate selectivity of human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
genetic analysis of MGAM, exon boundaries, and chromosome mapping
Raw starch granule degradation with recombinanat human MGAM indicates that pancreatic alpha-amylase hydrolysis is not a requirement for native starch digestion in the human small intestine.
Intestinal maltase-glycoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
Acarbose has been found to improve insulin levels and thus glucose/insulin ratios more effectively in overweight patients compared with nonoverweight patients with PCOS.
This study reported the first diagnosed Finnish patient with a phenotype compatible with the late-onset form of Pompe disease. Molecular genetic analysis of the GAA gene revealed a novel missense mutation (Y575X),combined with (P545L) mutation.
investigation of dietary control of Mgam expression in jejunum: high starch diet induces Mgam through mechanism involving increased acetylation of histones and increased binding of CREBBP, CDX2, and HNF1 to Mgam gene
The alpha-glucogenic activities of the jejunal mucosa with and without added recombinant pancreatic alpha-amylase, using a range of food starch substrates are reported.
mucosal alpha-glucogenic activity of Mgam plays a crucial role in the regulation of prandial glucose homeostasis
This gene encodes maltase-glucoamylase, which is a brush border membrane enzyme that plays a role in the final steps of digestion of starch. The protein has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities.
, brush border hydrolase
, maltase-glucoamylase, intestinal
, acid (Pompe disease, glycogen storage disease type II)
, acid alpha-glucosidase
, acid maltase
, glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)
, lysosomal alpha-glucosidase
, sucrase-isomaltase, intestinal