Anti-Anopheles gambiae Alpha Glucosidase [Agm3] Antibody
![Anti-Anopheles gambiae Alpha Glucosidase [Agm3] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1166_2001202001263711650.jpg "Anti-Anopheles gambiae Alpha Glucosidase [Agm3] Antibody")
This rabbit IgG polyclonal antibody was generated against a 30-kDa peptide corresponding to the C-terminus of Anopheles gambiae Alpha Glucosidase and recognizes A. gambiae Alpha Glucosidase.
Highlights:
- Reacts with A. gamiae Alpha Glucosidase
- Useful in R&D involving Anopheles, for identification and validation of targets for insect control by - d-endotoxins, and other biochemical/biological methods
- Several species of Anopheles are disease vectors (malaria, canine heartworm, filariasis, O’nyong’nyong)
- Recommended for Western Blot, Immunofluorescence, Immunohistochemistry and ELISA applications
Alpha-glucosidase is a glucosidase located on the brush border of the small intestine that acts upon 1,4-alpha bonds. The role of alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Deficiences in alpha glucosidase are associated with Pompe Disease and Diabetes.
From the laboratory of Michael J. Adang, PhD, University of Georgia.
Part of The Investigator's Annexe program.
This rabbit IgG polyclonal antibody was generated against a 30-kDa peptide corresponding to the C-terminus of Anopheles gambiae Alpha Glucosidase and recognizes A. gambiae Alpha Glucosidase.
Highlights:
- Reacts with A. gamiae Alpha Glucosidase
- Useful in R&D involving Anopheles, for identification and validation of targets for insect control by - d-endotoxins, and other biochemical/biological methods
- Several species of Anopheles are disease vectors (malaria, canine heartworm, filariasis, O’nyong’nyong)
- Recommended for Western Blot, Immunofluorescence, Immunohistochemistry and ELISA applications
Alpha-glucosidase is a glucosidase located on the brush border of the small intestine that acts upon 1,4-alpha bonds. The role of alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Deficiences in alpha glucosidase are associated with Pompe Disease and Diabetes.
From the laboratory of Michael J. Adang, PhD, University of Georgia.
Part of The Investigator's Annexe program.
| Product Type: | Antibody |
| Antigen: | alpha-glucosidase from A. gambiae(also referred to as: maltase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) |
| Accession ID: | P10253 |
| Molecular Weight: | 67 kDa |
| Isotype: | IgG |
| Clonality: | Polyclonal |
| Clone Name: | Anti-Agm3 |
| Reactivity: | A. gambiae. Very likely other members of the Anopheles genus, less likely Culex. Possibly, other insects/particularly mosquitoes |
| Immunogen: | Peptide |
| Species Immunized: | NZW Rabbit |
| Epitope: | C-terminal region (30-kDa peptide) |
| Purification Method: | Sepharose beads/ethanolamine buffer, pH 8 |
| Method Used to Determine Concentration: | Bio-Rad protein assay using bovine serum albumin (BSA) as standard |
| Buffer: | Na2CO3/NaHCO3, pH 9.6 |
| Tested Applications: | WB, IF, IHC, ELISA |
| Storage: | -80C |
| Shipped: | Dry ice |
- Zhang, Q., Hua, G., Bayyareddy, K., and Adang, M.J. 2013. Analyses of a-amylase and a-glucosidase in the malaria vector Anopheles gambiae as receptors of Cry11Ba toxins of Bacillus thuringiensis subsp. jegethesan. Insect Biochem. Mole. Biol. 31:907-915.
- Bayyareddy K1, Zhu X, Orlando R, Adang MJ. Proteome analysis of Cry4Ba toxin-interacting Aedes aegypti lipid rafts using geLC-MS/MS. J Proteome Res. 2012 Dec 7;11(12):5843-55.
- Bayyareddy K1, Andacht TM, Abdullah MA, Adang MJ. Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae. Insect Biochem Mol Biol. 2009 Apr;39(4):279-86.
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