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. Author manuscript; available in PMC: 2013 Aug 30.
Published in final edited form as: Arthritis Rheum. 2009 Oct;60(10):2902–2912. doi: 10.1002/art.24814

Figure 1. Characterization of specific antibodies against OPN-FL, OPN-R and OPN-L and development of specific ELISAs.

Figure 1

Recombinant human OPN-FL was digested with thrombin (IIa) or thrombin (IIa)/CPB to produce OPN-R and OPN-L respectively. A. Western blot analysis of human OPN-FL, OPN-R and OPN-L with the specific anti-peptide antibodies anti-OPN, anti-OPN-R and anti-OPN-L. OPN-R (SLAYGLR) and OPN-L (SVVYGL) peptides were used for competitive inhibition of antibody binding. B, ELISAs for OPN-FL (commercial), OPN-R and OPN-L ELISA. C. Competition of substituted peptides for binding of anti-OPN-R and anti-OPN-L to immobilized purified OPN-R and OPN-L respectively. Inhibition of binding by the cognate unsubstituted peptide was defined as 100%.