Anti-Anopheles gambiae Alkaline Phosphatase [AgALP1] Antibody

This rabbit IgG polyclonal antibody was generated against a peptide corresponding to amino acids 41-555 of Anopheles gambiae Alkaline phosphatase and recognizes A. gambiae Alkaline phosphatase.


  • Reacts with A. gamiae Alkaline phosphatase
  • 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

Alkaline phosphatases (ALPs, EC constitute a family of dimeric metalloenzymes that catalyze the hydrolysis of phosphate monoesters. ALPs play a role iphosphate uptake and transportmechanisms. They also may be important to the integrity of the brush border under environmental and pathogenic challenges.

From the laboratory of Michael J. Adang, PhD, University of Georgia.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
Anti-Anopheles gambiae Alkaline Phosphatase [AgALP1] Antibody
50uL Currently unavailable
Regular Price:$375.00
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Product Type: Antibody
Antigen: Alkaline phosphatase (AgALP1) from A. gambiae
Accession ID: P05186
Molecular Weight: 62.3 kDa
Isotype: IgG
Clonality: Polyclonal
Clone Name: Anti-AgALP1
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: A region of AgALP1 encoding amino acid residues 41-555 with a C-terminal Glu-Leu and a six-His tag
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

From the laboratory of Michael J. Adang, PhD, University of Georgia.
  1. Hua G, Zhang R, Bayyareddy K, Adang MJ. Anopheles gambiae alkaline phosphatase is a functional receptor of Bacillus thuringiensis jegathesan Cry11Ba toxin. Biochemistry. 2009 Oct 20;48(41):9785-93.

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