Recombinant human noggin protein
QK034
Brand: Qkine
Human noggin is a bone morphogenetic protein (BMP) antagonist which regulates cell differentiation and growth. Noggin is used in the culture of intestinal, pancreatic, lung and tumor-derived organoids and the maintenance of undifferentiated embryonic stem cells (ESC) and for stem cell differentiation into neural and microglial lineages.
Qkine human noggin (Qk034) is a highly pure, animal origin-free, bioactive 46 kDa dimer for reproducible results in organoid culture.

Currency:
Product name | Catalog number | Pack size | Price | Price (USD) | Price (GBP) | Price (EUR) |
---|---|---|---|---|---|---|
Recombinant human noggin protein, 25 µg | QK034-0025 | 25 µg | (select above) | $ 280.00 | £ 205.00 | € 240.00 |
Recombinant human noggin protein, 50 µg | QK034-0050 | 50 µg | (select above) | $ 410.00 | £ 305.00 | € 357.00 |
Recombinant human noggin protein, 100 µg | QK034-0100 | 100 µg | (select above) | $ 620.00 | £ 455.00 | € 532.00 |
Recombinant human noggin protein, 500 µg | QK034-0500 | 500 µg | (select above) | $ 2,500.00 | £ 1,840.00 | € 2,150.00 |
Recombinant human noggin protein, 1000 µg | QK034-1000 | 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
Species reactivity
Human
Species similarity:
mouse – 99%
rat – 99%
bovine – 99%
porcine – 99%
Frequently used together:
Summary
- High purity human noggin protein (Uniprot: Q13253)
- 46 kDa (dimer)
- >98%, by SDS-PAGE quantitative densitometry
- Expressed in E. coli
- Animal origin-free (AOF) and carrier protein-free
- Manufactured in Qkine's Cambridge, UK laboratories
- Lyophilized from acetonitrile, TFA
- Resuspend in 10 mM HCl (Reconstitution solution A) at >50 µg/ml, add carrier protein if desired, prepare single-use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term)
Featured applications
- Tumor organoid culture
- Epithelial organoid culture (WNR media)
- Stem cell differentiation into neural and microglial lineages
Bioactivity
Human noggin is a BMP inhibitor, and its activity is determined by inhibition of BMP-2 (Qk007) activity in a BMP-2 responsive firefly luciferase reporter assay. HEK293T cells are treated in triplicate with a serial dilution of noggin and a standard concentration of BMP-2 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 1.5 nM (70.1 ng/ml). Data from Qk034 lot #104291.
Purity
Noggin protein (Qk034) has an unusual migration in non-reduced (NR) SDS-PAGE due to the non-covalent dimer which is the active protein. Similar migration in SDS-PAGE is seen for gremlin-1, a related BMP antagonist. The identity of the purified dimeric protein was confirmed using mass spectrometry. Upon reduction, the protein monomer migrates at 23 kDa. Purified recombinant human noggin protein (7 μg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250. Data from Qk034 lot #104285.
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%
Qkine human noggin is as biologically active as a comparable alternative supplier protein. Quantitative luciferase assay with Qkine human noggin (Qk034, green) and alternative supplier noggin (Supplier B, black) inhibition of BMP-2 (Qk007). Cells were treated in triplicate with a serial dilution of noggin and a standard concentration of BMP-2 for 6 hours. Firefly luciferase activity was measured and normalized to control Renilla luciferase activity.
Protein background
Noggin is a 64 kDa homodimeric glycoprotein expressed during embryonic development and in adult cells [1]. Noggin is an extracellular antagonist of BMP cell signaling. BMPs are part of the larger TGFβ family and regulate embryonic, fetal and adult development in all vertebrates [1, 2]. Noggin binds to BMP-2, -4, -6 and -7, preventing interaction of the ligands with their receptor, and consequently blocking downstream activation of signaling cascades [2,3].
Through its control of BMP signaling, noggin plays a crucial role in embryonic patterning, as well as in the development of the neural tube, teeth, hair follicles, and the eye [4]. In cell cultures, noggin is used in the maintenance of pluripotent stem cells, differentiation of iPSCs to neural lineages, and in a large variety of organoid culture systems including intestine, liver and lung organoids [4, 5].
Background references
- Krause, C., Guzman, A. and Knaus, P. Noggin, Int. J. Biochem. Cell Biol., 43:4 (2011). doi.org/10.1016/j.biocel.2011.01.007.
- La Rosa, I., Camargo, L.S., Pereira, M.M. et al. Effects of bone morphogenic protein 4 (BMP4) and its inhibitor, Noggin, on in vitro maturation and culture of bovine preimplantation embryos. Reprod Biol Endocrinol 9:18 (2011). doi.org/10.1186/1477-7827-9-18.
- Rifas, L. The Role of Noggin in Human Mesenchymal Stem Cell Differentiation. J. Cell. Biochem. 100:824–834 (2007). doi.org/10.1002/jcb.21132.
- Urbischek, M., Rannikmae, H., Foets, T. et al. Organoid culture media formulated with growth factors of defined cellular activity. Sci Rep 9, 6193 (2019). doi.org/10.1038/s41598-019-42604-0
- Wang,G., Zhang, H., Zhao, Y., Li, J., Cai, J., Wang, P., Meng, S., Feng, J., Miao, C., Ding, M., Li, D. and Deng, H. Noggin and bFGF cooperate to maintain the pluripotency of human embryonic stem cells in the absence of feeder layers. Biochem Biophys Res Commun 330:3 (2005). doi.org/10.1016/j.bbrc.2005.03.058.
Publications using recombinant human noggin protein (Qk034)
Discovery and optimization of a guanylhydrazone-based small molecule to replace bFGF for cell culture applications
Feofanov M, Daubner GM, Saltalamacchia A et al.
DOI: https://doi.org/10.1101/2024.10.30.620903
Human epidermis organotypic cultures, a reproducible system recapitulating the epidermis in vitro
Agarwal R, Dittmar T, Beer HD et al.
DOI: 10.1111/exd.14823
Identification of molecular and functional subtypes using chronic pancreatitis patient-derived organoid models
Osorio-Vasquez V, Lumibao JC, Peck KL et al.
DOI: https://doi.org/10.1101/2024.10.30.620903
Spatial profiling of early primate gastrulation in utero
Bergmann S, Penfold CA, Slatery E et al.
DOI: 10.1038/s41586-022-04953-1
The effect of extracellular matrix on the precision medicine utility of pancreatic cancer patient-derived organoids
Lumibao JC, Okhovat SR, Peck KL et al.
DOI: 10.1172/jci.insight.172419