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Recombinant human GDF-5 protein (Qk070)

Growth differentiation factor 5 (GDF-5) plays a crucial role during embryonic development and tissue homeostasis and is specifically involved in the development of the skeletal system. Recombinant human GDF-5 protein is commonly used for the differentiation and maintenance of induced pluripotent stem cells, embryonic stem cells, or bone marrow-derived mesenchymal stem cells into osteoblasts and chondrocytes.

Human GDF-5 is a dimer with a molecular weight of 27 kDa. This protein is animal-free, carrier protein-free, and tag- free with exceptional lot-to-lot consistency. GDF-5 is suitable for reproducible and high-quality chondrocytes and osteoblasts.

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1000µg will be despatched as 2 x 500µg

Fast and free shipping.
Buy online with secure credit card or purchase order.
For any questions, please email orders@qkine.com

Summary

  • High-purity human protein (UniProt number: P43026)

  • >98%, by SDS-PAGE quantitative densitometry

  • Expressed in E. coli

  • 27 kDa monomer

  • Animal-free (AOF) and carrier protein-free

  • Manufactured in Cambridge, UK

  • Lyophilized from acetonitrile/TFA

  • Resuspend in 10 mM HCl, prepare single-use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C

Featured applications

  • Generation of iPSC-derived osteoblasts

  • Generation of iPSC-derived chondrocytes

  • Maintenance of mesenchymal stem cells

  • Differentiation of mesenchymal stem cells to chondrocytes

  • Differentiation of adipose-derived stromal cells to osteogenic lineages

Bone morphogenetic protein 14 (BMP-14)
Cartilage-derived morphogenetic protein 1 (CDMP-1)
Lipopolysaccharide-associated protein 4 (LAP-4; LPS-associated protein 4)
Radotermin

  1. Francis-West PH, Abdelfattah A, Chen P, Allen C, Parish J, Ladher R, et al. Mechanisms of GDF-5 action during skeletal development. Development. 1999 Mar 15;126(6):1305–15.
  2. Jin L, Li X. Growth Differentiation Factor 5 Regulation in Bone Regeneration. Curr Pharm Des. 2013 Jun 1;19(19):3364–73.
  3. Miyamoto Y, Mabuchi A, Shi D, Kubo T, Takatori Y, Saito S, et al. A functional polymorphism in the 5′ UTR of GDF5 is associated with susceptibility to osteoarthritis. Nat Genet. 2007 Apr;39(4):529–33.
  4. Storm EE, Kingsley DM. GDF5 Coordinates Bone and Joint Formation during Digit Development. Dev Biol. 1999 May 1;209(1):11–27.
  5. Nickel J, Kotzsch A, Sebald W, Mueller TD. A Single Residue of GDF-5 Defines Binding Specificity to BMP Receptor IB. J Mol Biol. 2005 Jun 24;349(5):933–47.
  6. Buxton P, Edwards C, Archer CW, Francis-West P. Growth/Differentiation Factor-5 (GDF-5) and Skeletal Development. JBJS. 2001 Mar;83(1):S23.
  7. Enochson L, Stenberg J, Brittberg M, Lindahl A. GDF5 reduces MMP13 expression in human chondrocytes via DKK1 mediated canonical Wnt signaling inhibition. Osteoarthritis Cartilage. 2014 Apr 1;22(4):566–77.
  8. Li X, Zheng Y, Zheng Y, Huang Y, Zhang Y, Jia L, et al. Circular RNA CDR1as regulates osteoblastic differentiation of periodontal ligament stem cells via the miR-7/GDF5/SMAD and p38 MAPK signaling pathway. Stem Cell Res Ther. 2018 Aug 31;9(1):232.
  9. Farng E, Urdaneta AR, Barba D, Esmende S, McAllister DR. The Effects of GDF-5 and Uniaxial Strain on Mesenchymal Stem Cells in 3-D Culture. Clin Orthop. 2008 Aug 1;466(8):1930–7.
  10. Hatakeyama Y, Tuan RS, Shum L. Distinct functions of BMP4 and GDF5 in the regulation of chondrogenesis. J Cell Biochem. 2004;91(6):1204–17.
  11. Colombier P, Clouet J, Boyer C, Ruel M, Bonin G, Lesoeur J, et al. TGF-β1 and GDF5 Act Synergistically to Drive the Differentiation of Human Adipose Stromal Cells toward Nucleus Pulposus-like Cells. Stem Cells. 2016 Mar 1;34(3):653–67.
  12. Zeng Q, Li X, Beck G, Balian G, Shen FH. Growth and differentiation factor-5 (GDF-5) stimulates osteogenic differentiation and increases vascular endothelial growth factor (VEGF) levels in fat-derived stromal cells in vitro. Bone. 2007 Feb 1;40(2):374–81.
  13. Zhang R, Yao J, Xu P, Ji B, Luck JV, Chin B, et al. A comprehensive meta-analysis of association between genetic variants of GDF5 and osteoarthritis of the knee, hip and hand. Inflamm Res. 2015 Jun 1;64(6):405–14.
  14. Faiyaz-Ul-Haque M, Ahmad W, Zaidi S, Haque S, Teebi A, Ahmad M, et al. Mutation in the cartilage-derived morphogenetic protein-1 (CDMP1) gene in a kindred affected with fibular hypoplasia and complex brachydactyly (DuPan syndrome). Clin Genet. 2002;61(6):454–8.
  15. Kania K, Colella F, Riemen AHK, Wang H, Howard KA, Aigner T, et al. Regulation of Gdf5 expression in joint remodelling, repair and osteoarthritis. Sci Rep. 2020 Jan 13;10(1):157.
  16. Polinkovsky A, Robin NH, Thomas JT, Irons M, Lynn A, Goodman FR, et al. Mutations in CDMP1 cause autosomal dominant brachydactyly type C. Nat Genet. 1997 Sep;17(1):18–9.
  17. Thomas JT, Lin K, Nandedkar M, Camargo M, Cervenka J, Luyten FP. A human chondrodysplasia due to a mutation in a TGF-β superfamily member. Nat Genet. 1996 Mar;12(3):315–7.

Bioactivity

Bioactivity graph showing the EC50 of ng/ml (pM) for Qkine recombinant GDF-5

GDF-5 activity is determined using the GDF-5-responsive firefly luciferase reporter assay. Transfected HEK293T cells are treated in triplicate with a serial dilution of GDF-5 for 24 hours. Firefly luciferase activity is measured and normalised to the control Renilla luciferase activity. Data from Qk070 lot #204571.

 EC50 = 7.2 ng/mL (0.53 nM).

Purity

SDS-PAGE gel showing the high purity reduced and non-reduced forms of GDF-5

Recombinant GDF-5 migrates as a major band at approximately 27 kDa in non-reduced conditions (NR). Upon reduction (R), only the monomer band at approximately 13.5 kDa is visible. No contaminating protein bands are present.

The purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk070 batch #204571.

Further quality assays

  • Mass spectrometry, single species with the expected mass

  • Endotoxin: <0.005 EU/μg protein (below the level of detection)

  • Recovery from stock vial: >95%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Protein background

Growth differentiation factor 5 (GDF-5) belongs to the transforming growth factor beta (TGF-β) superfamily and is closely related to the bone morphogenetic proteins (BMPs) subfamily [1]–[4]. GDF-5 plays a crucial role during embryonic development and tissue homeostasis and is specifically involved in the development of the skeletal system, where it promotes the formation and maintenance of bones and joints [1], [2]. GDF-5 regulates the proliferation and differentiation of the osteoblasts (osteogenesis) and chondrocytes (chondrogenesis)[2].

GDF-5, like other members of the TGF-β superfamily, is characterized by a conserved structure consisting of a signal peptide, prodomain, and a mature domain [5]. The mature domain, responsible for the biological activity of the protein, contains a cysteine knot motif formed by six conserved cysteine residues [5]. GDF-5 binds to membrane-bound serine-/threonine-kinase receptors, termed type I and type II receptors, regulating downstream intracellular signaling pathways similarly to other members of TGF-β superfamily [2], [5]. GDF-5 activates Smad-dependent and Smad-independent pathways (MAPK, PI3K, and Wnt/β-catenin pathways) to regulate cellular processes such as development, growth, and survival [5]–[8].

GDF-5 is commonly in cell culture for the differentiation and maintenance of induced pluripotent stem cells, embryonic stem cells, or bone marrow-derived mesenchymal stem cells. It promotes the differentiation to osteoblasts and chondrocytes when used with BMP-4 [1], [2], [6], [9], [10]. Additionally, GDF-5 is used with TGF-β1 to stimulate osteogenic differentiation of adipose-derived stromal cells [11], [12].

Mutations in the GDF-5 gene have been associated with various skeletal disorders [3], [5], [13]. For example, loss-of-function mutations in GDF-5 have been linked to congenital disorders such as Hunter-Thompson syndrome, brachydactyly type C, and DuPan syndrome [14]–[17]. On the other hand, polymorphisms in the GDF-5 gene have been associated with an increased risk of developing osteoarthritis, a degenerative joint disease [3], [13]. Manipulating GDF-5 activity could offer novel therapeutic strategies for promoting bone and joint regeneration or for mitigating the progression of diseases affecting these tissues.

Our products are for research use only and not for diagnostic or therapeutic use.  Products are not for resale.

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