Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | 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). |
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Source | Mouse myeloma cell line, NS0-derived human Noggin protein
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Accession # | |||||||
N-terminal Sequence | No results obtained: Gln28 predicted |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | NOG |
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Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 49.6 kDa (monomer). 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. |
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SDS-PAGE | 58-62 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
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).
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