Recombinant Murine NOGGIN (rMuNOGGIN)

SKU:BHP11300482
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    Overview
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    Recombinant NOGGIN Mouse protein. Produced in E. coli. Suitable for functional assays, binding studies, and cell-based research.
    Expression System E. coli
    Purity >95% by SDS-PAGE and HPLC analyses.
    Endotoxin LAL-Tested
    Molecular Weight Approximately 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
    Physical Form Lyophilized Powder
    Available Options

    Select the variant that best fits your experiment. Availability and lead time may vary by option.

    • Options — Size: 1 mg / 5 ug / 20 ug
    • Lead time: options listed in “Availability Content”; other statuses may take longer.
    • Storage: This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for…
    • Shipping: cold-chain shipment with dry ice or blue ice packs.
    • Upon receipt: store at recommended temperature as soon as possible.
    • Sales terms and conditions: Please review prior to ordering.
    Options selector
    Catalog no. Size
    PR2032-1MG 1 mg
    PR2032-5UG 5 ug
    PR2032-20UG 20 ug
    Field Specification
    Biological Activity Determined by its ability to inhibit 5.0 ng/ml of BMP-4 induced alkaline phosphatase production by ATDC chondrogenic cells. The expected ED50 for this effect is 1.0-2.0 ng/ml of Noggin, corresponding to a Specific Activity of >5 x 105 IU/mg.
    Endotoxin Level Less than 1EU/mg of rMuNOGGIN as determined by LAL method.
    Formulation Lyophilized from a 0.2μm filtered concentrated solution in 30% acetonitrile, 0.1% TFA.
    Molecular Weight Approximately 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
    Product Type
    • Recombinant Protein
    Purity >95% by SDS-PAGE and HPLC analyses.
    Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
    Source Escherichia coli
    Storage This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

    Scientific Background

    Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14.

    Product Description

    E. coli Expression

    Recombinant NOGGIN Mouse protein is produced using a validated E. coli expression system and supplied as lyophilized powder for long-term stability. Suitable for use in functional bioassays, ELISA standard curves, receptor binding studies, antibody validation, and related research applications.

    Protein Specifications

    Expression System E. coli
    Molecular Weight Approximately 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
    Purity >95% by SDS-PAGE and HPLC analyses.
    Endotoxin Less than 1EU/mg of rMuNOGGIN as determined by LAL method.
    Physical Form Sterile Filtered White lyophilized (freeze-dried) powder.
    Formulation Lyophilized from a 0.2μm filtered concentrated solution in 30% acetonitrile, 0.…
    Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
    Storage This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, …
    ✓ Purity Verified by SDS-PAGE
    ✓ LAL Endotoxin-Tested

    Functional Activity

    Determined by its ability to inhibit 5.0 ng/ml of BMP-4 induced alkaline phosphatase production by ATDC chondrogenic cells. The expected ED50 for this effect is 1.0-2.0 ng/ml of Noggin, corresponding to a Specific Activity of >5 x 105 IU/mg.

    Safety & Handling

    This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China

    What expression system was used and why does it matter?

    This protein was produced in E. coli expression system. Expression system selection determines glycosylation profile, folding, and post-translational modifications. For cell-based stimulation assays, verify the expression system matches the glycosylation requirements of your target receptor or pathway.

    How do I reconstitute this protein?

    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions. Reconstitute in sterile distilled water or PBS at 100 µg/mL as a standard starting concentration. Allow to dissolve at 4°C for 30 minutes without vortexing. Prepare working aliquots in 0.1% BSA carrier protein and store at −80°C.

    What is the biological activity of this protein?

    This protein has been validated for functional bioactivity: Determined by its ability to inhibit 5.0 ng/ml of BMP-4 induced alkaline phosphatase production by ATDC chondrogenic cells. The expected ED50 for this effect is 1.0-2.0 ng/ml of Noggin, corresponding to a Specific Activity of >5 x 105 IU/mg.. Optimal working concentrations may vary depending on your cell type, assay format, and culture conditions. Titrate the protein in a dose-response experiment to determine the optimal concentration for your system.

    What is the endotoxin level and why does it matter for cell-based assays?

    Endotoxin level is Less than 1EU/mg of rMuNOGGIN as determined by LAL method. as determined by the LAL method. Low endotoxin is critical for cell-based studies because endotoxin activates NF-κB and TLR4 signalling in immune cells, producing artefactual cytokine induction that can completely mask the true biological activity of the recombinant protein.

    What are the recommended storage conditions?

    This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. F Upon receipt, immediately store at −80°C. Prepare single-use working aliquots to avoid repeated freeze-thaw cycles. Lyophilized protein is stable for 6–12 months at −80°C from the date of receipt.

    BioHippo offers flexible sourcing options for qualified research institutions and partners. The following may be available subject to supplier capabilities and order volume.

    • Custom quantities: Bulk pricing or non-standard sizes available for high-throughput screening or scale-up projects.
    • Custom formulation: Alternative reconstitution buffers or carrier proteins may be accommodated on request.
    • Extended QC data: Additional bioactivity assay data, endotoxin reports, or SEC-HPLC purity profiles available on request.

    Contact BioHippo customer support to discuss your requirements.

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