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Recombinant Human Noggin, Animal-Free Protein

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Human Noggin is a BMP inhibitor, and its activity is determined by inhibition of BMP2 (Qk007) activity in a BMP-2 responsive firefly luciferase reporter assay. HEK293T cells are treated in triplicate with a serial ...read more
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 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Catalog# & Formulation Size Price

Recombinant Human Noggin, Animal-Free Protein Summary

Details of Functionality
No significant difference between EC50 of reference and test lots
Source
E. coli-derived human Noggin protein
Accession #
Protein/Peptide Type
Animal-Free Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
46 kDa (dimer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
Oligomeric human Noggin protein only

Packaging, Storage & Formulations

Storage
Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
Buffer
Lyophilized from acetonitrile/TFA
Reconstitution Instructions
Resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Noggin, Animal-Free Protein

  • NOG
  • Noggin
  • SYM1
  • symphalangism 1 (proximal)
  • synostoses (multiple) syndrome 1
  • SYNS1
  • SYNS1A

Background

Noggin is a secreted homodimeric glycoprotein that is an antagonist of bone morphogenetic proteins (BMPs) (1, 2). Human Noggin cDNA encodes a 232 amino acid (aa) precursor protein; cleavage of a 19 aa signal peptide generates the 213 aa mature protein which contains an N-terminal acidic region, a central basic heparin‑binding segment and a C-terminal cysteine-knot structure (2). Secreted Noggin probably remains close to the cell surface due to its binding of heparin‑containing proteoglycans (3). Noggin is very highly conserved among vertebrates, such that mature human Noggin shares 99%, 99%, 98%, 97% and 89% aa sequence identity with mouse, rat, bovine, equine and chicken Noggin, respectively. Noggin binds some BMPs such as BMP-4 with high affinity and others such as BMP-7 with lower affinity. It antagonizes BMP bioactivities by blocking epitopes on BMPs that are needed for binding to both type I and type II receptors (2, 4). During embryogenesis, Noggin antagonizes specific BMPs at defined times, for example, during neural tube, somite and cardiomyocyte growth and patterning (5-7). During skeletal development, Noggin prevents chondrocyte hyperplasia, thus allowing proper formation of joints (4). Mutations within the cysteine-knot region of human Noggin are linked to multiple types of skeletal dysplasias that result in apical joint fusions (8). Noggin is expressed in defined areas of the adult central nervous system and peripheral tissues such as lung, skeletal muscle and skin (1). During culture of human embryonic stem cells (hESC) or neural stem cells under certain conditions, addition of Noggin to antagonize BMP activity may allow stem cells to proliferate while maintaining their undifferentiated state, or alternatively, to differentiate into dopaminergic neurons (6, 9 - 13). Noggin also appears to maintain adult stem cell populations in-vivo, for example, maintaining neural stem cells within the hippocampus (13).

  1. Valenzuela, D.M. et al. (1995) J. Neurosci. 15:6077.
  2. Groppe, J. et al. (2002) Nature 420:636.
  3. Paine-Saunders, S et al. (2002) J. Biol. Chem. 277:2089.
  4. Brunet, L. J. et al. (1998) Science 280:1455.
  5. McMahon, J. A. et al. (1998) Genes Dev. 12:1438.
  6. Itsykson, P. et al. (2005) Mol. Cell. Neurosci. 30:24.
  7. Yuasa, S. et al. (2005) Nat. Biotechnol. 23:607.
  8. Gong, Y. et al. (1999) Nat. Genet. 21:302.
  9. Xu, R.-H. et al. (2005) Nat. Methods 2:185.
  10. Wang, G. et al. (2005) Biochem. Biophys. Res. Commun. 330:934.
  11. Chaturvedi, G. et al. (2009) Cell Prolif. 42:425.
  12. Chiba, S. et al. (2008) Stem Cells 26:2810.
  13. Bonaguidi, M.A. et al. (2008) J. Neurosci. 28:9194.

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