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Recombinant Human Maltase-glucoamylase (MGAM), partial

Recombinant Human Maltase-glucoamylase (MGAM), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

MGAM

Uniprot NO.

O43451

Alternative Names

4-alpha-glucosidase; Alpha-glucosidase; Glucan 1; Glucoamylase; Maltase-glucoamylase; intestinal; MGA; MGA_HUMAN; MGAM; MGAML

Species

Homo sapiens (Human)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Buffer

Lyophilized from Tris/PBS-based buffer, 6% Trehalose, pH 8

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.

Gene References into Functions

Mechanistic Pathway on Human alpha-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations PMID:29548257
MGAM, or nearby regulatory elements, may be involved in the etiology of oral clefts. PMID:25776870
Starch internal structure modulates its susceptibility to MGAM. The internal branch amounts negatively affect the glucose release rate. PMID:25037326
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. PMID:22563462
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 PMID:22036121
we report crystal structures of C-terminal maltase-glucoamylase alone at a resolution of 3.1 angstroms, and in complex with its inhibitor acarbose PMID:22058037
analysis of substrate selectivity of human maltase-glucoamylase and sucrase-isomaltase N-terminal domains PMID:20356844
genetic analysis of MGAM, exon boundaries, and chromosome mapping PMID:12547908
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. PMID:17485087
Intestinal maltase-glycoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. PMID:18036614
Acarbose has been found to improve insulin levels and thus glucose/insulin ratios more effectively in overweight patients compared with nonoverweight patients with PCOS. PMID:18377903
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. PMID:19472353