N17001 Sigma

Noggin human

recombinant, expressed in HEK 293 cells, suitable for cell culture

Synonym: Noggin human



recombinant   expressed in HEK 293 cells
assay   ≥98% (SDS-PAGE)
form   lyophilized powder
potency   ≤10 ng/mL ED50
mol wt   mol wt 23 kDa (The protein migrates as a 25 kDa band on SDS-PAGE due to glycosylation)
suitability   suitable for cell culture
storage temp.   −20°C


Analysis Note

The biological activity of recombinant human noggin was tested in culture by measuring its ability to inhibit BMP4-induced alkaline phosphatase production by ATDC5 cells (human erythroleukemic indicator cell line).
The EC50 is defined as the effective concentration of growth factor that elicits a 50% decrease in alkaline phosphatase secretion in a cell based bioassay.

Physical form

Supplied as a lyophilized powder containing phosphate buffered saline.

Biochem/physiol Actions

Noggin is a secreted protein that inhibits the binding of bone morphogenetic proteins (BMPs) to their cognate receptor. It is a 232 amino acid-secreted glycosylated protein, which forms covalently linked homodimers and has high affinity for BMP4. hESC cultured with noggin (in medium or incorporated into extracellular matrix) form denser colonies compared to normal hESC cultures, suggesting that the presence of noggin promotes better growth. Noggin can be incorporated as a medium supplement for maintaining stem cells in a pluripotent state, for short-term culture experiments. Noggin does not trigger differentiation towards a neuronal lineage. Furthermore, when incorporated into extracellular matrix, noggin prevented spontaneous differentiation during the time period examined. In a surgically induced knee osteoarthritis model in mice, expression of noggin mRNA was lost from the articular cartilage, which correlated with loss of BMP2/4 and pSMAD1/5/8, an indicator of active BMP signaling.

General description

Recombinant human Noggin is expressed in human 293 cells as a glycoprotein with a calculated molecular mass of 23 kDa. This protein is manufactured in human cells using an all-human production system, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports better stability of the protein in culture.



Price and Availability

Cultivate Regeneration
Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 
Protocols & Articles


Growth Factors in Stem Cell Biology

Growth factors are naturally occurring regulatory molecules, which bind to receptors on the cell surface. They stimulate cell and tissue function through influencing cell differentiation by changing ...
Keywords: Adhesion, Angiogenesis, Cell biology, Cell proliferation, Cellular processes, Diseases, Growth factors, Hormones, Stem cell biology, Therapeutic uses, Transcription, Transfection

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