Noggin Recombinant

SKU:BHP18201774
Research Validated
Suppliers
BPS Bioscience
BPS Bioscience
Details Products
Overview
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Recombinant Noggin Human protein. Spanning aa 28-232(end). Produced in Mammalian (HEK293). Suitable for binding assays, inhibitor screening, and drug discovery.
Expression System Mammalian (HEK293)
Biosafety Level BSL-1
Expression Region aa 28-232(end)
UniProt ID Q13253
Options selector
Catalog no. Size
90256-1 5 ug
90256-2 20 ug
Available Options

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

  • Options — Size: 5 ug / 20 ug
  • Lead time: options listed in “Availability Content”; other statuses may take longer.
  • Storage: ≥12 months (lyophilized) at -20°C. Store reconstituted protein in aliquots at -2…
  • Shipping: Shipped at -80°C (dry ice) (dry ice).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No 90256
Alternative Names Noggin, symphalangism 1, SYM1, synostoses (multiple) syndrome 1, SYNS1
Biological Activity Measured by Noggin's ability to inhibit BMP-4-induced alkaline phosphatase production by C2C12 mouse myoblast cells. The ED50 is <20 ng/ml in the presence of 30 ng/ml of human BMP-4.
Endotoxin Level <1 EU/µg (Noggin, by LAL method)
Formulation Lyophilized from a 0.2 µm filtered 0.1 mg/ml solution of 50 mM Tris, pH 8.0, 1.2 M NaCl, 2.7 mM KCl, 0.1% BSA
Molecular Weight 28 kDa
Product Type
  • Recombinant Protein
Reconstitution Reconstitute in sterile water with 0.1% BSA to a final concentration of 0.1 mg/ml. Final formulation will be 50 mM Tris, pH 8.0, 1.2 M NaCl, 2.7 mM KCl, 0.1% BSA. This solution can then be diluted into other buffers. To maximize product collection from vial surface, vortex briefly and then spin down to recollect the liquid.
Shipping -80°C (dry ice)
Species Human
Storage ≥12 months (lyophilized) at -20°C. Store reconstituted protein in aliquots at -20°C to -70°C for up to 6 months. Avoid freeze/thaw cycles.
UniProt # Q13253

Scientific Background

Noggin is one of a group of proteins that act as secreted antagonists of BMP activity. BMPs are essential for osteogenesis and organogenesis during embryonic development, and also play a role in tissue healing in adults. Noggin inhibits BMP activity by binding to them with high affinity, blocking their ability to bind to their receptor.

Product Description

Mammalian (HEK293) Expression

Recombinant Noggin Human protein is produced using a validated Mammalian (HEK293) expression system and supplied in aqueous buffer solution. Suitable for enzyme kinetics, inhibitor screening, binding assays, structural studies, and related biochemical research applications.

Protein Specifications

UniProt ID Q13253
Expression System Mammalian (HEK293)
Amino Acids / Region 28-232(end)
Molecular Weight 28 kDa
Endotoxin <1 EU/µg (Noggin, by LAL method)
Formulation Lyophilized from a 0.2 µm filtered 0.1 mg/ml solution of 50 mM Tris, pH 8.0, 1.2…
Storage ≥12 months (lyophilized) at -20°C. Store reconstituted protein in aliquots at -2…
Biosafety Level Not applicable (BSL-1)
✓ Purity Verified
✓ Endotoxin-Tested

Safety & Handling

Avoid freeze/thaw cycles.

What expression system was used and why does it matter for enzymatic activity?

This protein was produced in Mammalian (HEK293). Expression system selection determines post-translational processing, disulfide bond formation, and co-factor incorporation — all of which affect enzymatic activity. Insect cell (Sf9) systems are preferred for kinases and multi-subunit enzymes that require phosphorylation or chaperone assistance; E. coli is used for structurally simpler proteins.

What amino acid region is included in this construct?

This protein spans amino acids 28-232(end). Confirm the region includes your domain of interest — the active site, binding pocket, or substrate recognition sequence — before placing your order. Refer to the UniProt database for domain annotation.

What is the purity and how was it verified?

Purity is assessed by SDS-PAGE; see the Certificate of Analysis. A gel image is provided with each lot. BPS Bioscience performs rigorous QC on each lot, including purity assessment and functional activity testing where applicable. Contact technical support if purity ≥99% is required for biophysical measurements.

What applications is this protein suitable for?

Useful for cell culture and for the study of signaling and developmental pathways. Also useful for receptor binding studies, screening inhibitors, and selectivity profiling. Refer to the product datasheet for validated protocols and recommended assay conditions. Contact BioHippo technical support for application-specific guidance.

How should this protein be stored and handled?

≥12 months (lyophilized) at -20°C. Store reconstituted protein in aliquots at -20°C to -70°C for up to 6 months. Avoid freeze/thaw cycles. Avoid repeated freeze-thaw cycles — prepare single-use working aliquots. Add BSA or glycerol to aliquots if storing diluted enzyme is necessary. Typical stability is at least 6 months at −80°C.

BioHippo offers flexible sourcing for qualified research institutions and partners.

  • Bulk quantities: Large-scale orders for HTS campaigns or structural studies.
  • Custom constructs: Alternative tag positions, truncation variants, or point mutants may be available upon request.
  • Biotinylated variants: Avi-Tag site-specific biotinylation is available for SPR/BLI surface capture applications.
  • Extended QC data: Activity assay data, SEC-HPLC profiles, or additional purity methods available on request.

Contact BioHippo customer support for custom requirements.

  1. Tao, Y.X., et al. (2010). Indian J. Exp. Biol. 48(5):444-52.
  2. Mfopou, J.K., et al. (2010). Gastroenterology. 138(7):2233-2245.
  3. Chaturvedi, G., et al. (2009). Cell Prolif. 42(4):425-33
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Experience the power of Celltrypse™, c-LEcta's innovative enzyme solution for gentle and efficient cell dissociation. Request your free sample and discover a superior alternative for your cell culture workflows.

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