What factor can enhance the stability of GFP during purification?

Maintaining cold temperatures or adding stabilizers significantly enhances the stability of GFP during purification by mitigating the effects of thermal denaturation and proteolytic degradation. Lower temperatures slow down enzymatic reactions and protein aggregation, which are common concerns during protein purification processes. Likewise, stabilizers can provide an environment that maintains protein structure and function by preventing denaturation and aggregation.

High concentrations of salt can sometimes lead to protein precipitation rather than stabilization, while heating proteins is typically counterproductive as it can cause denaturation. Adding more fluorescent markers does not contribute to protein stability in the same way; instead, it may complicate the purification process without providing structural support to the GFP itself. Thus, the combination of cold temperatures and stabilizers is a well-established strategy to optimize the stability of GFP during purification efforts.