Anti-Ovalbumin (chicken, denatured)
Mouse monoclonal antibody
Cat.No. HYB 094-05
Preparation: Protein-A purified
Content: Available in 200 µL and 1 mL volumes, 1 mg/mL
Solvent: 0.01 M phosphate buffer, pH 7.4, containing 0.5 M NaCl and 15mM sodium azide Storage: In the dark at 4-8ºC
Ovalbumin is the main protein found in egg white, making up 60-65% of the total protein. Native chicken ovalbumin is a globular monomer with a molecular mass of 45 kDa (1). It is structurally related to both serpins and lipocalins.
Purified chicken ovalbumin was treated with formaldehyde and lysine for 2 weeks at 35ºC and the autoclaved for 1 h at 110ºC (2) before being adsorbed onto aluminum hydroxide gel.
HYB 094-05 reacts with denatured ovalbumin. Cross-reactivity with ovalbumins from other avian species has not been tested.
Epitope specificity differs from that of HYB 094-06 and HYB 094-07,as indicated by lack of mutual inhibition of antigen binding.
HYB 094-05 reacts with chicken ovalbumin in denatured or modified forms (surface-adsorbed, heat-denatured or reduced), including native chicken ovalbumin coated directly onto the microtiter well (3). In Western blotting after SDS-PAGE, HYB 094-05 reacts with ovalbumin in both reduced and unreduced forms.
| Method | Usability | Dilution guideline | References |
| ELISA | Yes | 1/25,000 | |
| Immunoblotting | Yes | 1/2000 | |
| Immunohistochemistry | Not determined |
The dilution guideline for ELISA is based on use as detection antibody for native ovalbumin coated at 10 µg/mL. Users should determine the optimal dilutions for their own purposes.
1. Nisbet AD, Saundry RH, Moir AJ, Fothergill LA, Fothergill JE (1981) The complete amino acid sequence of hen ovalbumin. Eur J Biochem 115:335-345.
2. Koch C, Jensen SS, Oster A, Houen G (1996) A comparison of the immunogenicity of the native and denatured forms of a protein. APMIS 104:115-125.
3. Houen G, Koch C (1997) A non-denaturing enzyme linked immunosorbent assay with protein preadsorbed onto aluminum hydroxide. J Immunol Methods 200:99-105.
