NOG Protein (AA 28-232)
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- Target Alle NOG Proteine anzeigen
- NOG (Noggin (NOG))
- Protein-Typ
- Recombinant
- Biologische Aktivität
- Active
- Proteineigenschaft
- AA 28-232
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Spezies
- Human
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Quelle
- CHO Cells
- Produktmerkmale
- ED50<2.5 ng/mL, measured in a bioassay using ATDC5 cells in the presence of 10 ng/mL human BMP-4.
- Reinheit
- > 95 % as analyzed by SDS-PAGE.
- Endotoxin-Niveau
- < 0.2 EU/μg, determined by LAL method.
- Top Product
- Discover our top product NOG Protein
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- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Lyophilized
- Rekonstitution
- Reconstituted in ddH2O or PBS at 100 μg/mL.
- Buffer
- Lyophilized after extensive dialysis against PBS.
- Lagerung
- -80 °C
- Informationen zur Lagerung
- Lyophilized recombinant human Noggin remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, human Nogginshould be stable up to 1 week at 4°C or up to 2 months at -20°C.
- Haltbarkeit
- 6 months
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- Target
- NOG (Noggin (NOG))
- Andere Bezeichnung
- Noggin (NOG Produkte)
- Synonyme
- SYM1 Protein, SYNS1 Protein, nog-A Protein, nog1 Protein, noggin-1 Protein, noggin Protein, noggin Protein, noggin L homeolog Protein, noggin protein Protein, NOG Protein, Nog Protein, nog.L Protein, noggin Protein
- Hintergrund
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Noggin, also known as NOG, is a homodimeric glycoprotein that bindsto and modulates the activity of TGF-beta family ligands. It is expressed in condensing cartilage and immature chondrocytes. Noggin antagonizes bone morphogenetic protein (BMP) activities by blocking epitopes on BMPs needed for binding to their receptors. Noggin has been shown to be involved in many developmental processes, such as neural tube formation and joint formation. During development, Noggin diffuses through extracellular matrices and forms morphogenic gradients, regulating cellular responses dependent on the local concentration of the signaling molecule.
Synonyms: NOG - Molekulargewicht
- 29-31kDa, observed by reducing SDS-PAGE.
- UniProt
- Q13253
- Pathways
- Stem Cell Maintenance, Tube Formation
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