Anti-Anopheles gambiae Aminopeptidase [AgAPN2] Antibody
![Anti-Anopheles gambiae Aminopeptidase [AgAPN2] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1164_2001202001263611630.jpg "Anti-Anopheles gambiae Aminopeptidase [AgAPN2] Antibody")
This rabbit IgG polyclonal antibody was generated against a peptide corresponding to amino acids 228-843 of Anopheles gambiae Aminopeptidase and recognizes A. gambiae Aminopeptidase.
Highlights:
- Reacts with A. gamiae Aminopeptidase
- 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
Aminopeptidase is an enzyme that catalyzes the breakdown of a peptide, removing the amino acyl residue at the amino end of the chain (that is, an N-exopeptidase); found in intestinal secretions. They are widely distributed throughout both animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components.
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 peptide corresponding to amino acids 228-843 of Anopheles gambiae Aminopeptidase and recognizes A. gambiae Aminopeptidase.
Highlights:
- Reacts with A. gamiae Aminopeptidase
- 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
Aminopeptidase is an enzyme that catalyzes the breakdown of a peptide, removing the amino acyl residue at the amino end of the chain (that is, an N-exopeptidase); found in intestinal secretions. They are widely distributed throughout both animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components.
From the laboratory of Michael J. Adang, PhD, University of Georgia.
Part of The Investigator's Annexe program.
Specifications
| Product Type: | Antibody |
| Antigen: | Aminopeptidase from A. gambiae |
| Molecular Weight: | 106 kDa |
| Isotype: | IgG |
| Clonality: | Polyclonal |
| Clone Name: | Anti-AgAPN2 |
| 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: | 70-kDa peptide encoding amino acid residues 228 to 843 |
| 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 |
Provider
From the laboratory of Michael J. Adang, PhD, University of Georgia.
References
- Zhang, R., Hua, g., Andacht, T.M., and Adang, M.J. 2008. A 106-kDa aminopeptidase is a putative receptor for Bacillus thuringiensis Cry11Ba toxin in the mosquito Anopheles gambiae genome. Biochemistry. 47(43). 11263-11272.
- Zhang, R., Hua, G., Urbauer, J.L., and Adang, M.J. (2010) Synergistic and inhibitory effects of aminopeptidase peptides on Bacillus thuringiensis Cry11Ba toxicity in the mosquito Anopheles gambiae. Biochemistry. 49(39):8512-9.
If you publish research with this product, please let us know so we can cite your paper.
