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- Ab02791-23.0 Anti-Deoxycholic acid [Ab #88]
- Species independent
- Rabbit IgG
- Purified
- Ships in 4-5 weeks
- Ab02791-1.1 Anti-Deoxycholic acid [Ab #88]
- Species independent
- Mouse IgG1
- Purified
- In Stock
Recombinant monoclonal antibody to Deoxycholic acid. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma Ab #88.
Alternative Name(s) of Target: DCA; ChEBI:28834
Immunogen: The original antibody was generated by immunizing mice with a conjugated of deoxycholic acid and bovine serum albumin (BSA).
Specificity: This antibody is binds deoxycholic acid. It is also capable of detecting N-ε-deoxycholyl lysine. Deoxycholic acid is a bile acid. Deoxycholic acid is one of the secondary bile acids, which are metabolic byproducts of intestinal bacteria.
Application Notes: To characterize this antibody, an ELISA was performed on HRP conjugated deoxycholic acid and on standard bile acid solution using the mouse IgG1 version of this antibody. This antibody is capable of sensitive detection of DCA residues (270 femtograms) anchored on BSA molecules. Furthermore the mouse IgG1 version of this antibody was used for immunoaffinity extraction of DCA-introduced peptide (Kobayashi et al, 2000). The scFv version of this antibody was generated to be used as a probe to monitor DCA residues anchored on proteins. In a competitive enzyme-linked immunosorbent assay using DCA-coated microtiter plates, the scFv provided a dose-response curve for free DCA ranging between 2 and 5000 pg/assay. This scFv could also monitor trace amounts of DCA residues anchored on a protein through DCA acyl adenylate reactions, the likely reactive intermediate (Kobayashi et al, 2005; pmid:15784283).
Antibody first published in:
Kobayashi et al. Production of a monoclonal antibody for sensitive monitoring of deoxycholic acid residues anchored on endogenous proteins. Analytical sciences, 2000, vol 16 PMID:
Note on publication:
A monoclonal antibody which recognizes deoxycholic acid (DCA) residues anchored on endogenous proteins was generated.