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Recombinant human GDF-15 protein

QK017

Brand: Qkine

Human growth differentiation factor 15 (GDF-15) protein is a member of the TGFβ family and subject of intense interest as a marker of cellular stress and for its role in metabolism, cancer and pregnancy.  Human GDF-15 also is functional in mouse studies.

Qkine GDF-15 is a 25 kDa disulfide-linked dimer composed of the mature domain of human GDF-15 protein. Our recombinant GDF-15 protein is exceptionally high purity, animal origin-free and extensively validated to ensure no trace contamination of related TGF-β family proteins from the mammalian culture systems.

Qkine 3-for-2 product campaign

Currency: 

Product name Catalog number Pack size Price Price (USD) Price (GBP) Price (EUR)
Recombinant human GDF-15 protein, 25 µg QK017-0025 25 µg (select above) $ 280.00 £ 205.00 € 240.00
Recombinant human GDF-15 protein, 50 µg QK017-0050 50 µg (select above) $ 410.00 £ 305.00 € 357.00
Recombinant human GDF-15 protein, 100 µg QK017-0100 100 µg (select above) $ 620.00 £ 455.00 € 532.00
Recombinant human GDF-15 protein, 500 µg QK017-0500 500 µg (select above) $ 2,500.00 £ 1,840.00 € 2,150.00
Recombinant human GDF-15 protein, 1000 µg QK017-1000 1000 µg (select above) $ 3,950.00 £ 2,900.00 € 3,388.00

Note: prices shown do not include shipping and handling charges.

Qkine company name and logo are the property of Qkine Ltd. UK.

Alternative protein names
Growth/differentiation factor 15, Macrophage inhibitory cytokine 1 (MIC 1), NSAID activated gene 1 protein (NAG1)
Species reactivity

human

species similarity:
mouse – 67%
porcine – 67%
rat – 66%
bovine – 66%


Summary

  • High purity human GDF-15 protein (Uniprot: Q99988)
  • >98%, by SDS-PAGE quantitative densitometry
  • 25 kDa (dimer). Mature active protein is a disulfide-linked dimer.
  • Expressed in E. coli
  • Animal origin-free (AOF)
  • Carrier protein-free
  • Manufactured in Qkine's Cambridge, UK laboratories
  • Lyophilized from acetonitrile, TFA
  • Resuspend in 10 mM HCl at >100 µg/ml (provided with protein and free of charge), prepare single use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C
Handling and Storage FAQ

Featured applications

  • Biomarker for cellular stress
  • In vivo metabolic studies in mice (using human GDF-15)

Bioactivity

Human GDF15 Qk017 protein purity SDS-PAGE lot #011

GDF-15 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 GDF-15, in particular those purified from mammalian expression systems, have been shown previously to be contaminated with trace amounts of TGF-β. These trace contaminants cause misleading experimental results due to the picomolar or even femtomolar EC50s (Olsen et al., 2017). Here we use a well-characterized SMAD2/3 activation assay to show that there is no contamination from other TGF-β family proteins. Bioactivity is determined using a luciferase reporter assay in HEK293T cells.  Cells are treated (in triplicate) with a serial dilution of GDF-15 or Qk010 TGF-β1 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 0 pM (no contamination with TGF-β or related growth factors). Data from Qk017 lot #104282

Purity

Human GDF15 Qk017 protein purity SDS-PAGE lot #011

GDF-15 migrates as a single band at 24 kDa in non-reducing (NR) and 13 kDa as a single monomeric species upon reduction (R).  No contaminating protein bands are visible. Purified recombinant protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.  Data from Qk017 lot #010

Further quality assays

  • Mass spectrometry: single species with expected mass
  • Analytical reversed-phase: single sharp peak
  • Endotoxin: <0.005 EU/μg protein (below level of detection)
  • Recovery from stock vial:  >95%

Protein background

Growth differentiation factor 15 (GDF-15) is a distant member of the TGF-β superfamily. Its expression is tightly regulated and circulating GDF-15 protein in serum is associated with diseases such as cancer, cardiovascular disease, obesity and metabolic disease. GDF-15 protein is being recognized as an important biomarker for cellular stress.

Unlike other members of the TGF-β superfamily that cause activation of the SMAD pathway, GDF-15 protein signals through GRAL and co-receptor RET leading to RET phosphorylation and signalling through the ERK and AKT pathway [1]. Commercial sources of recombinant human GDF-15 protein, in particular those purified from mammalian expression, are frequently contaminated with trace amounts of TGF-β 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-characterized SMAD2/3 activation assay to confirm there is no SMAD signalling.

Background references

  1. Emmerson, P. J., Duffin, K. L., Chintharlapalli, S. & Wu, X. GDF15 and Growth Control. Front. Physiol. 9, 1712 (2018). doi: 10.3389/fphys.2018.01712
  2. Olsen, O. E., Skjærvik, A., Størdal, B. F., Sundan, A. & Holien, T. TGF-β contamination of purified recombinant GDF15. PLoS One 12, e0187349 (2017). doi.org/10.1371/journal.pone.0187349

Publications using recombinant human GDF-15 protein (Qk017)

Activation of the hypothalamic–pituitary–adrenal axis by exogenous and endogenous GDF15
In PNAS on 29 June 2021 by Cimino, I. et al.
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GDF15 linked to maternal risk of nausea and vomiting during pregnancy
In Nature on 13 December 2023 by Fejzo, M., Rocha, N., Cimino, I. et al.
View publication

Fetally-encoded GDF15 and maternal GDF15 sensitivity are major determinants of nausea and vomiting in human pregnancy
Preprint 4 June 2023 by Fejzo, M. et al.
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The Common H202D Variant in GDF-15 Does Not Affect Its Bioactivity but Can Significantly Interfere with Measurement of Its Circulating Levels
In The Journal of Applied Laboratory Medicine November 2022 by Karusheva, Y. et al.
View publication