Drosophila peroxidasin is an extracellular matrix-associated peroxidase (Horikoshi et al., 1999 [PubMed 10441517]). It is expressed exclusively in hemocytes derived from head mesoderm at a very early stage of differentiation. Peroxidasin exists as a homotrimer with a unique hybrid structure that combines an enzymatically functional peroxidase domain with motifs that are typically found in extracellular matrix-associated proteins. It is a secreted protein that contains a secretory recognition sequence at its N terminus. Peroxidasin catalyzes hydrogen peroxide-driven radioiodination, oxidations, and the formation of dityrosine in vitro. It is also thought to function in extracellular matrix consolidation, phagocytosis, and defense.
Host: Rabbit Target: PXDN Positive control (+): MCF7 (N10) Negative control (-): THP-1 (N30) Antibody concentration: 3ug/ml
Surface Plasmon Resonance Kinetic Characterization of Polyclonal Antibody Affinity. Purified polyclonal antibodies were immobilized on a Protein A/G coated Carterra LSA sensor chip (PAGH200M) at concentrations of 5, and 50 ug/mL in duplicate. Antibodies on the surface were exposed to interaction with peptides sequentially via microfluidic controlled flow at 333nM peptide concentration for kinetic characterization of the binders for affinity and specificity, followed by curve fitting using the Kinetics software. Kd determinations for both concentrations were averaged and results and standard deviation are shown.
PXDN Antibody - N-terminal region (ARP42360_P050) in Human COLO205 using Western Blot
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