Noggin Human, Sf9
Sf9, Baculovirus cells.
SYM1, SYNS1, NOG.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE.
Description
Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).
Noggin is purified by proprietary chromatographic techniques.
Product Specs
Noggin, a protein encoded by the NOG gene, plays a crucial role in regulating bone morphogenetic proteins (BMPs), particularly BMP-4, by binding and inhibiting their signaling activity. Its ability to efficiently diffuse through extracellular matrices allows it to establish morphogenic gradients, influencing embryonic development and later-stage processes. Originally identified in Xenopus for its role in restoring dorsal-ventral axis formation, Noggin's importance is further emphasized by mouse knockout studies demonstrating its involvement in neural tube fusion and joint formation. In humans, dominant NOG mutations have been linked to skeletal disorders such as proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). These mutations affect highly conserved amino acid residues, highlighting the significance of Noggin's structure and function across species. The amino acid sequence of human Noggin exhibits a high degree of similarity to its counterparts in Xenopus, rat, and mouse.
Produced in Sf9 insect cells using a baculovirus expression system, this recombinant Noggin is a glycosylated homodimer, composed of two identical subunits. Each subunit contains 205 amino acids, contributing to a total molecular mass of 47.9 kDa under non-reducing conditions. Notably, during SDS-PAGE analysis, the apparent molecular size may range from 50 to 80 kDa due to glycosylation. The purification process involves proprietary chromatographic techniques ensuring high purity.
This product appears as a sterile, white powder obtained through lyophilization (freeze-drying).
This product has been lyophilized from a concentrated solution (0.2μm filtered) in phosphate-buffered saline (PBS) at pH 7.4, containing 0.02% Tween-20 and 5% trehalose as stabilizing agents.
To reconstitute the lyophilized Noggin, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Lyophilized Noggin remains stable for 3 weeks when stored at room temperature. However, for long-term storage, it is recommended to store the desiccated product at temperatures below -18°C. Once reconstituted, Noggin should be stored at 4°C for a period of 2-7 days. For extended storage, aliquot and store at temperatures below -18°C. Repeated freezing and thawing should be avoided to maintain protein integrity and activity.
The purity of this product is greater than 95%, as determined by two independent analytical methods: reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
The biological activity of this product is assessed by its ability to inhibit BMP-4-induced alkaline phosphatase production in ATDC5 mouse chondrogenic cells. The concentration of Recombinant Human Noggin required to achieve this effect is typically in the range of 0.04-0.2 μg/mL in the presence of 50 ng/mL Recombinant Human BMP-4.
SYM1, SYNS1, NOG.
Sf9, Baculovirus cells.
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.
Product Science Overview
Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids, with a molecular mass of approximately 47.9 kDa under non-reducing conditions . The molecular size on SDS-PAGE appears at approximately 50-80 kDa . This recombinant form of Noggin is optimized for use in cell culture, differentiation studies, and functional assays .
Noggin’s primary function is to inhibit BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells . The effective dose (ED50) for this inhibition is less than 3 ng/ml, corresponding to a specific activity of 3.3x10^5 units/mg . This inhibition is crucial for regulating developmental processes such as neural tube fusion and joint formation .
Recombinant human Noggin has a wide range of applications in scientific research, including:
- Differentiation Studies: It is used to differentiate embryonic stem (ES) and induced pluripotent stem (iPS) cells into neural stem cells and retinal cells .
- Tissue Engineering: Noggin is involved in the differentiation of human ES and iPS cell-derived endodermal lineages .
- Adipogenic Differentiation: It induces adipogenic differentiation of mesenchymal stem cells (MSCs) .
Mutations in the NOG gene are associated with several bone diseases, including proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) . These conditions are characterized by multiple joint fusions and map to the same region (17q22) as the NOG gene . The amino acid sequence of human Noggin shows high homology across several species, including Xenopus, rat, and mouse .
Lyophilized Noggin is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage . Upon reconstitution, it should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use . It is recommended to add a carrier protein (0.1% HSA or BSA) to prevent freeze-thaw cycles .
