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Mouse Anti-MGAM Antibody (HBB2/143/17) (CBMAB-1427CQ)

This product is a mouse antibody that recognizes MGAM. The antibody HBB2/143/17 can be used for immunoassay techniques such as: ELISA, IF, IHC, IP.
See all MGAM antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
HBB2/143/17
Antibody Isotype
IgG1
Application
ELISA, IF, IHC, IP

Basic Information

Immunogen
Purified intestinal brush border membrane from normal adult human jejunal mucosa
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Supernatant
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
MGAM
Introduction
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. Diseases associated with MGAM include Diarrhea and Hypomagnesemia 1, Intestinal. Among its related pathways are Metabolism and Galactose metabolism.
Entrez Gene ID
8972
UniProt ID
O43451
Alternative Names
MG; MGA
Function
Alpha-(1,4) exo-glucosidase involved in breakdown of dietary starch oligosaccharides in small intestine. Cleaves the non-reducing alpha-(1,4)-linked glucose residue in linear dextrins with retention of anomeric center stereochemistry (PubMed:12547908, PubMed:18356321, PubMed:27480812, PubMed:18036614, PubMed:22058037).

Mainly hydrolyzes short length oligomaltoses having two to seven glucose residues (PubMed:12547908, PubMed:18356321, PubMed:27480812, PubMed:18036614, PubMed:22058037).

Can cleave alpha-(1,2), alpha-(1,3) and alpha-(1,6) glycosidic linkages with lower efficiency, whereas beta glycosidic linkages are usually not hydrolyzed (PubMed:27480812).
Biological Process
Dextrin catabolic process Source: UniProtKB
Maltose catabolic process Source: UniProtKB
Starch catabolic process Source: ProtInc
Cellular Location
Plasma membrane
Apical cell membrane
Note: Brush border.
Topology
Cytoplasmic: 1-13
Helical: 14-34
Lumenal: 35-2753
PTM
N- and O-glycosylated.
Does not undergo intracellular or extracellular proteolytic cleavage.
Sulfated.

Tannous, S., Stellbrinck, T., Hoter, A., & Naim, H. Y. (2023). Interaction between the α-glucosidases, sucrase-isomaltase and maltase-glucoamylase, in human intestinal brush border membranes and its potential impact on disaccharide digestion. Frontiers in Molecular Biosciences, 10, 1160860.

Guan, S., Han, X., Li, Z., Xu, X., Cui, Y., Chen, Z., ... & Li, H. (2022). Exploration of the Interactions between Maltase–Glucoamylase and Its Potential Peptide Inhibitors by Molecular Dynamics Simulation. Catalysts, 12(5), 522.

Zhang, S., Wang, Y., Han, L., Fu, X., Wang, S., Li, W., & Han, W. (2021). Targeting N-terminal human maltase-glucoamylase to unravel possible inhibitors using molecular docking, molecular dynamics simulations, and adaptive steered molecular dynamics simulations. Frontiers in Chemistry, 9, 711242.

Dong, Y. S., Yu, N., Li, X., Zhang, B., Xing, Y., Zhuang, C., & Xiu, Z. L. (2020). Dietary 5, 6, 7-trihydroxy-flavonoid aglycones and 1-deoxynojirimycin synergistically inhibit the recombinant maltase–glucoamylase subunit of α-glucosidase and lower postprandial blood glucose. Journal of Agricultural and Food Chemistry, 68(33), 8774-8787.

Mehraban, M. H., Mansourian, M., Ahrari, S., HajiEbrahimi, A., Odooli, S., Motovali-Bashi, M., ... & Ghasemi, Y. (2019). Maltase-glucoamylase inhibition potency and cytotoxicity of pyrimidine-fused compounds: An in silico and in vitro approach. Computational Biology and Chemistry, 82, 25-36.

Awdishu, L., Tsunoda, S., Pearlman, M., Kokoy-Mondragon, C., Ghassemian, M., Naviaux, R. K., ... & RamachandraRao, S. P. (2019). Identification of maltase glucoamylase as a biomarker of acute kidney injury in patients with cirrhosis. Critical care research and practice, 2019.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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