Recombinant human GDF15
Growth/differentiation factor 15 (GDF15) is a distant member of the TGFβ superfamily (Uniprot: Q99988). Its expression is tightly regulated and circulating GDF15 in serum is associated with diseases such as cancer, cardiovascular disease, obesity and metabolic disease.
Unlike other members of the TGFβ superfamily that cause activation of the SMAD pathway, GDF15 signals through GRAL and co-receptor RET leading to RET phosphorylation and signalling through the ERK and AKT pathway (reviewed in Emmerson et al., 2018). Commercial sources of GDF15, in particular those purified from mammalian expression are frequently contaminated with trace amounts of TGFβ and related proteins. These trace contaminants cause misleading experimental results due to the picomolar or even femtomolar EC50s of this family of cytokines (2).
We produce our proteins in E.coli with no animal products in our culture or purification processes to ensure there is no contamination from related proteins. In addition, we use a well-characterised SMAD2/3 activation assay to confirm there is no SMAD signalling.
Alternative protein names: Growth/differentiation factor 15, Macrophage inhibitory cytokine 1 (MIC 1), NSAID activated gene 1 protein (NAG1)
Summary: Qk015 Mature domain of human GDF15 (Uniprot: Q99988) expressed in E.coli and purified to homogeneity. Mature active protein is a disulphide-linked dimer.
Form: protein is provided lyophilised from a fully volatile solution without carrier protein.
Molecular mass: ~25 kDa (for the dimer)
Quality testing: all our proteins are made in-house by our scientists. We take the quality of our proteins very seriously and you can view the full quality testing data for each batch of protein by clicking on the link below
GDF15 is very poorly soluble in physiological solutions, so we would recommend following the handling guidance for lyophilised cytokines instructions closely. To minimise loss of protein due to precipitation or adsorption to plastic, we advise storing the recombinant protein at very low pH to before dilution in cell culture media. Low pH will also assist in maintaining the correct disulphide structure of the protein by minimising disulphide bond exchange reactions.
Every effort is made to ensure samples are sterile however we recommend sterile filtering after dilution in media or the final working solution.
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Recombinant mature domain of human activin A protein (residues 311-426, Uniprot: P08476) expressed in E.coli (animal-derived component free). Protein supplied lyophilised with no carrier protein present. Activin A is used in stem cell maintenance and differentiation.