Recombinant human noggin protein

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

Purity

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

1. 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.
2. 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.
3. 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.
4. 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
5. 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