Immunoprecipitation (IP) is a widely used method for protein purification as well as for studying protein-protein interactions. The commercially available Protein A/G agarose beads are commonly used for immunoprecipitation (IP) applications, but they are expensive and require cold-chain storage. This makes them inaccessible for many resource-limited laboratories. In this proposal, we aim to develop a cost-effective, cellulose-based solid-phase matrix for IP applications. Our strategy involves covalent antibody immobilization onto the cellulose surface by first introducing amine groups through silanization using 3-aminopropyltriethoxysilane (APS), followed by crosslinking with glutaraldehyde via Schiff base formation. The unreacted aldehyde group on the surface-bound glutaraldehyde remains available to form covalent bonds with the N-terminal amine groups of antibodies, enabling stable immobilization.