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Human Noggin Protein (E. coli), Research Grade
Research use only

  • This product is designed for academic and scientific research institutions.
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Cat. No. / Size
Price
Qty
NON-H5118-20ug
$140.00
NON-H5118-50ug
$190.00
NON-H5118-1mg (500ug X 2)
$1570.00
ETA of in-stock products:2 business days
Sub-Total$ 0

Product Details

  • Features and Advantages

    1. Native Conformation: Native sequences, tag-free and natural function.
    2. Reliable Activity: Biological activity calibrated against WHO/NIBSC standards.
    3. Stringent Quality Control: Protein content, purity, and cell-based bioactivity testing for each batch.
    4. Lowest Endotoxin level (<0.01 EU/ug).
    5. Safety Assurance: Sterile filtration through 0.2 μm membrane.
    6. AOF: Animal origin-free raw materials throughout the production process.
  • Synonym

    Noggin, NOG, SYM1, SYNS1

  • Source

    Human Noggin Protein (E. coli), Research Grade (NON-H5118) is expressed from E. coli cells. It contains AA Gln 28 - Cys 232 (Accession # Q13253-1).

    Predicted N-terminus: Met

  • Molecular Characterization

    Noggin Structure

    Other Tags and Version Biotin & Other Labeled Version

    This protein carries no "tag".

    The protein has a calculated MW of 23.2 kDa. The protein migrates as 25 kDa±3 kDa under reducing (R) condition, and 65 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under non-reducing (NR) condition (SDS-PAGE).

  • Endotoxin

    Less than 0.01 EU per μg by the LAL method / rFC method.

  • Purity

    >95% as determined by SDS-PAGE.

    >95% as determined by SEC-HPLC.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 20 mM NaAc, pH4.5 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 24 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process
  • Quality Description

    ACRO's Research-grade products are suitable for a wide range of cell culture applications, particularly for research use in academic institutions. These products are sterilized by filtration, followed by lyophilization where applicable. Typical specifications include endotoxin levels of <0.01 EU/μg and purities >95%. Biological activity is calibrated against WHO/NIBSC standards when available.
    ACRO's Premium-grade (Pre-GMP) products are characterized by their high quality and enhanced safety profiles, making them ideal for early-stage discovery and manufacturing processes in cell therapy companies. A key advantage is their seamless transition to corresponding GMP-grade versions. Biological activity is calibrated against WHO/NIBSC standards when available. Typical specifications include endotoxin levels of <0.01 EU/μg and purities >95%. In addition, rigorous testing is conducted to ensure the absence of mycoplasma, HCD, and HCP, thereby guaranteeing product safety.

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Performance Data

  • SDS-PAGE

    Noggin SDS-PAGE

    Human Noggin Protein (E. coli), Research Grade on SDS-PAGE under reducing (R) and non-reducing (NR) conditions. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

  • SEC-HPLC

    Noggin SEC-HPLC

    The purity of Human Noggin Protein (E. coli), Research Grade (Cat. No. NON-H5118) was greater than 95% as determined by SEC-HPLC.

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Background

Noggin is also known as NOG, SYM1, SYNS1 and is a secreted homodimeric glycoprotein whose scaffold contains a cystine-knot topology similar to that of BMPs.Secreted Noggin probably remains close to the cell surface due to its binding of heparincontaining proteoglycans.Noggin inhibits TGF-β signal transduction by binding to TGF-β family ligands and preventing them from binding to their corresponding receptors. Noggin plays a key role in neural induction by inhibiting BMP4, along with other TGF-β signaling inhibitors such as chordin and follistatin. Mouse knockout experiments have demonstrated that noggin also plays a crucial role in bone development, joint formation, and neural tube fusion. During embryogenesis, Noggin antagonizes specific BMPs at defined times, for example, during neural tube, somite and cardiomyocyte growth and patterning. During skeletal development, Noggin prevents chondrocyte hyperplasia, thus allowing proper formation of joints. During culture of human embryonic stem cells (hESC) or neural stem cells under certain conditions, addition of Noggin to antagonize BMP activity may allow stem cells to proliferate while maintaining their undifferentiated state, or alternatively, to differentiate into dopaminergic neurons Noggin also appears to maintain adult stem cell populations in vivo, for example, maintaining neural stem cells within the hippocampus.

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