A major challenge in protein and vaccine storage is maintaining function during transport and avoiding cold-chain management, which is costly and energy-intensive. This study presents a novel method for storing and delivering proteins using a stiff, supramolecular hydrogel that prevents thermal denaturation and allows mechanical release of pure, excipient-free protein from a syringe. The hydrogel can hold up to 10 wt% of macromolecules without affecting release. Unlike existing methods, this approach does not require chemical triggers for release and ensures that only protein and buffer are delivered, avoiding the need for additional excipients. The hydrogel is formed by the self-assembly of low-molecular-weight gelators, which create a three-dimensional network that physically traps proteins, preventing irreversible aggregation. When pressure is applied, the gel is mechanically released through a syringe filter, resulting in a homogeneous, functional protein solution. This method is scalable, practical, and suitable for low-resource settings. The hydrogel was tested with various proteins, including insulin and β-galactosidase, showing that they retain function even at high temperatures. The method also demonstrated robustness under real-world conditions, such as shipping through postal services. This approach offers a promising solution for the cold-chain-free, cost-effective delivery of biologics worldwide.A major challenge in protein and vaccine storage is maintaining function during transport and avoiding cold-chain management, which is costly and energy-intensive. This study presents a novel method for storing and delivering proteins using a stiff, supramolecular hydrogel that prevents thermal denaturation and allows mechanical release of pure, excipient-free protein from a syringe. The hydrogel can hold up to 10 wt% of macromolecules without affecting release. Unlike existing methods, this approach does not require chemical triggers for release and ensures that only protein and buffer are delivered, avoiding the need for additional excipients. The hydrogel is formed by the self-assembly of low-molecular-weight gelators, which create a three-dimensional network that physically traps proteins, preventing irreversible aggregation. When pressure is applied, the gel is mechanically released through a syringe filter, resulting in a homogeneous, functional protein solution. This method is scalable, practical, and suitable for low-resource settings. The hydrogel was tested with various proteins, including insulin and β-galactosidase, showing that they retain function even at high temperatures. The method also demonstrated robustness under real-world conditions, such as shipping through postal services. This approach offers a promising solution for the cold-chain-free, cost-effective delivery of biologics worldwide.