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Recombinant human GDF15 protein
Qk017 Recombinant human GDF15 protein is a 25 kDa disulphide-linked dimer composed of the mature domain of human growth differentiation factor 15 protein. Our recombinant GDF15 protein is expressed in E. coli and extensively validated to ensure no trace contamination of TGFβ, which can cause misleading results.
Qk017 Recombinant human GDF15 protein
Growth differentiation factor 15 (GDF-15) is a distant member of the TGFβ superfamily. Its expression is tightly regulated and circulating GDF15 protein in serum is associated with diseases such as cancer, cardiovascular disease, obesity and metabolic disease. GDF15 protein is being recognized an important biomarker for cellular stress.
Unlike other members of the TGFβ superfamily that cause activation of the SMAD pathway, GDF15 protein 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 recombinant human GDF15 protein, 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). Please be cautious with your source of recombinant GDF15 protein, our scientists are happy to provide further information, please email email@example.com
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-characterized SMAD2/3 activation assay to confirm there is no SMAD signalling.
Summary: Qk015 Mature domain of human GDF15 protein (Uniprot: Q99988) expressed in E. coli and purified to homogeneity. Mature active protein is a disulfide-linked dimer.
Molecular mass: ~25 kDa (for the dimer)
Form: protein is provided lyophilized from a fully volatile solution without carrier protein.
Purity and bioactivity
For peace of mind that our recombinant human GDF15 protein will work exactly the same way every day, from batch to batch and at any scale you need, we conduct extensive purity and bioactivity analysis. This includes SDS-PAGE, mass spectrometry, reverse phase chromatography, UV spectroscopy and endotoxin level testing.
To confirm the biochemical identity of our recombinant human GDF15 protein and ensure that its purity meets are rigorous standards, we conduct SDS-PAGE on every protein batch. As GDF-15 is a disulfide-linked dimer, we use both reduced and non-reduced conditions, as well as appropriate high sensitivity stains, for our SDS-PAGE analysis.
In the past, recombinant GDF15 protein from commercial suppliers was contaminated with endogeneous TGF beta family growth factors. Our production methods and careful elimination of any potential sources of contamination ensure a highly pure protein. We confirm this in a sensitive firefly luciferase reporter assay in HEK293T cells.
Find out more about our extensive purity testing in the next tab.
Protein purity: SDS-PAGE in reduced and non-reduced conditions
Bioactivity: we use a well characterized SMAD2/3 activation assay to show that there is no contamination from other TGFβ family proteins.