Maynard et al. have developed synthetic polymers with trehalose side chains for protein stabilization, enabling both freeze-drying and heating stabilization, but the conjugation reduces activity. However, for many therapeutic applications, covalent conjugation of a polymer using multistep synthetic chemistry and purification is not practical and has the requirement to seek regulatory approvals for each material, significantly increasing the barrier to clinical translation. This is a broad issue that means any stored protein is eventually delivered mixed with its stabilization agents, rather than the desirable solution of protein in buffer. Fully reversible hydrogels based on PEG (polyethylene glycol) have emerged to protect diverse proteins against thermal stress and mRNA formulations have been stabilized in a dissolvable matrix. Similarly, frozen formulations to prevent ice crystal growth suppress protein aggregation. However, in each case these gels are based upon new chemical entities (and hence a significant barrier to human use), may require a chemical stimulus (pH, sugars) to release the protein, which in practice must be dosed by the user, and take more than 1 hour to release the protein. Whilst potent, these strategies result in protein mixed with gel-forming components, which require separate approval and rigorous evaluation of their safety profile before being suitable for human use. Even materials based on PEG have immunological concerns for frequent exposure. An ideal biologic storage/transport solution would i) remove/reduce cold chain requirements; ii) be broadly applicable; iii) have zero or minimal excipients in the delivered protein solution; iv) not require complex chemical triggers to release; v) tolerate high loadings up to 100 mg/mL. Here we solve each of these points using a simple, low resource strategy. We show that low molecular weight supramolecular gel networks can physically entrap proteins preventing irreversible aggregation, and hence retain function at temperatures as high as 50°C for at least 4 weeks. Upon pushing out of the syringe through a filter, pure non-aggregated homogeneous and functional protein is released with all excipients trapped in the filter, ensuring only protein and buffer are delivered.