IgY - egg yolk antibody
 

IgY - main low molecular weight immunoglobulin present in hen's serum and egg yolk in concentration of around 5-20 mg/ml

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Molecular mass [kDa] ~ 180 (light chain ~ 25 [kDa] each; heavy chain ~ 65-68 [kDa] each) }
• Isoelectric point 5.7 - 7.6 (6.6 +/- 0.9 Davalos-Patoja et al. 2000)
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Extinction coefficient (i.e. absorbance of a 10 mg/ml solution at 280 nm) are: in 0.3 M KCl=13.18; in 0.1 N NaOH=14.4; in 5M guanidine=12.7
(Leslie and Clem 1969)

 

Name IgY has been proposed by Leslie and Clem in 1969. The authors showed experimental data proving that IgY molecule is different from IgG ("Phylogeny of immunoglobulin structure and function" G. A. Leslie and L.W. Clem, Journal of Experimental Medicine, Vol. 130, No. 6: 1337-1352, 1969).

Other names for IgY (often misleading) met in literature are: Chicken IgG, Egg Yolk IgG, 7SIgG.

Some interesting features of IgY:
 

• does not bind to rheumatoid factor (an inflammatory response marker) in blood (Larsson et al. 1988)
• does not activate mammalian complement factors (Larsson et al. 1992)
This can be of a great advantage in case of assay development for mammalian serum samples
• does not bind to cell surface Fc receptor ( Schmidt et al. 1993)
• does not bind to protein A (Kronvall et al. 1974) or protein G (Akerström et al. 1985)
• latex particles sensitized by IgY molecules do not aggregate by means of the rheumatoid factor (as is the case of IgG antibodies). Moreover IgY-latex complexes have higher colloidal stability than IgG at pH 8 (L.Davalos-Pantoja et al. 2000)
• IgY antibodies are selectively, in large amounts passed to egg yolk and therefore NO IgM and IgA impurities can be found in IgY preparations (Schade et al. 2001)
• might bind three to five times more secondary antibody ( Horton et al. 1984)
 

Goat Antibody
 

• We are ready to produce antibody against antigens in goat.