Expression of the RNA binding protein CIRP is up regulated in mammalian cells upon perception of mild cold shock (27-32^oC), conditions that can result in improved recombinant protein yields, improved protein folding and activity.  CIRP also binds to key proteins involved in the control of mRNA translation initiation, potentially acting as a bridge between the RNA and protein synthesis machinery. CIRP has two domains, an N-terminal RNA binding domain and an arginine/glycine rich C-terminal domain that is natively disordered. The N-terminal domain includes two RNA-binding sites, RNP1 and RNP2 that are conserved across many RNA binding proteins. RNA binding of the N-terminal domain has been investigated by introducing mutations into the RNP1 and RNP2 sites and monitoring subsequent RNA binding using electromobility shift assays and NMR. These studies confirm that specific residues in these regions are important for RNA interaction. Cell lines stably expressing CIRP have also been generated to further investigate the function of CIRP and to determine binding partners. These cell lines with manipulated CIRP levels have also been used to assess the influence of CIRP on recombinant protein production. Here we report on a structure-function based understanding of CIRP and how this information can be used to develop new strategies for enhanced recombinant protein expression from mammalian cells grown at mildly hypothermic temperatures.