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Recombinant Human Noggin Fc Chimera Protein, CF Best Seller

R&D Systems, part of Bio-Techne | Catalog # 3344-NG

R&D Systems, part of Bio-Techne
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3344-NG-050
3344-NG-100
3344-NG-500

Key Product Details

Source

NS0

Accession #

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Noggin protein
Human Noggin
(Gln28-Cys232)
Accession # Q13253
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

No results obtained: Gln28 predicted

Predicted Molecular Mass

49.6 kDa (monomer)

SDS-PAGE

58-62 kDa, reducing conditions

Activity

Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells.
The ED50 for this effect is 0.100-0.400 µg/mL in the presence of 30 ng/mL of Recombinant Human BMP‑4 (Catalog # 314-BP).

Scientific Data Images for Recombinant Human Noggin Fc Chimera Protein, CF

Graph showing bioactivity of human Noggin protein

Bioactivity of Human Noggin

Recombinant human Noggin Fc chimera (3344-NG) inhibits recombinant human BMP-4-induced alkaline phosphatase production in the ATDC5 mouse chondrogenic cell line. The ED50 for this effect is 0.100-0.400 µg/mL in the presence of 30 ng/mL of recombinant human BMP-4 (314-BP).

Formulation, Preparation and Storage

3344-NG
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Noggin

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, antagonizing 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 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) without feeder layers or conditioned medium, but with addition of FGF basic, addition of Noggin to antagonize BMP activity allows hESC to maintain their undifferentiated, pluripotent state (9, 10). In differentiation protocols, Noggin has been used to create neural crest stem cells from induced pluripotent stem cells (11). 

Because of its importance in the development of tissues, regenerative medicine utilizes Noggin to generate cells for intestinal tissues or organoids in vitro (12). Noggin is also an important factor for stimulating bone development and has neuroprotective effects in early stages of spinal cord injury (13, 14). Expression of Noggin can help contain or reduce metastatic lesions by limiting BMP signaling, making it a therapeutic option for cancer treatment (15). Noggin has been used to create bladder cancer organoids that can serve as a tissue model in preclinical testing of chimeric antigen receptor (CAR)-T-cell immunotherapy (16).

References

  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. Abe, R. et al. (2021) J. Rural. Med. 16:143.
  12. Kim, S. et al. (2022) Nat. Commu. 13:1692.
  13. Malijauskaite, S. et al. (2021) Cytokines Growth Factor Rev. 60:76.
  14. Al-Sammarraie, N. et al. (2022) Neural Regen Res. 18:492.
  15. Davis, H. et al. (2016) Cytokines Growth Factor Rev. 27:81.
  16. Yu, L. et al. (2021) Clin. Transl. Immunology 10:e1248.

Alternate Names

NOG, SYM1, SYNS1, SYNS1A

Entrez Gene IDs

9241 (Human); 18121 (Mouse)

Gene Symbol

NOG

UniProt

Additional Noggin Products

Product Documents for Recombinant Human Noggin Fc Chimera Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Noggin Fc Chimera Protein, CF

For research use only

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