Recombinant FGF-8,Human

SKU:BHP11300035
Suppliers
Bioworld Technology Inc
Bioworld Technology Inc
Details Products
Overview
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Recombinant FGF-8 Human protein. Produced in E. coli. ED50 < 5.0 ng. Suitable for functional assays, binding studies, and cell-based research.
Expression System E. coli
Purity > 95% by SDS-PAGE and HPLC analyses
Biological Activity ED50 < 5.0 ng
Endotoxin LAL-Tested
Molecular Weight 22.5kDa
Physical Form Lyophilized Powder
Options selector
Catalog no. Size
BK0044-10UG 10 ug
BK0044-50UG 50 ug
BK0044-1MG 1 mg
Available Options

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

  • Options — Size: 10 ug / 50 ug / 1 mg
  • Lead time: options listed in “Availability Content”; other statuses may take longer.
  • Storage: Lyophilized recombinant human Fibroblast Growth Factor-8 (rhFGF-8) remains stabl…
  • 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.
Field Specification
Mfr No BK0044
Biological Activity ED50 < 5.0 ng/ml, measured by a cell proliferation assay using 3T3 cells in the presence of 1μg/ml of heparin, corresponding to a specific activity of > 2.0× 10ˆ5 units/mg.
Endotoxin Level < 0.2 EU/μg, determined by LAL method.
Formulation Lyophilized after extensive dialysis against PBS.
Molecular Weight 22.5kDa, observed by reducing SDS-PAGE.
Product Type
  • Recombinant Protein
Purity > 95% by SDS-PAGE and HPLC analyses.
Reconstitution Reconstituted in ddH2O at 100 μg/ml.
Source Escherichia coli
Storage Lyophilized recombinant human Fibroblast Growth Factor-8 (rhFGF-8) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-8 should be stable up to 2 weeks at 4°C or up to 3 months at -20°C.

Scientific Background

Fibroblast Growth Factor-8 (FGF-8) is a heparin-binding growth factor of the FGF family. There are 4 known forms of FGF8 produced by alternative splicing: FGF8a, FGF-8b, FGF-8e and FGF-8f. The human and mouse FGF8b are identical of aa sequences. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF-8 is required for normal brain, eye, ear and limb development during embryogenesis.

Product Description

E. coli Expression

Recombinant FGF-8 Human 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 22.5kDa, observed by reducing SDS-PAGE.
Purity > 95% by SDS-PAGE and HPLC analyses.
Endotoxin < 0.2 EU/μg, determined by LAL method.
Physical Form Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized after extensive dialysis against PBS.
Reconstitution Reconstituted in ddH2O at 100 μg/ml.
Storage Lyophilized recombinant human Fibroblast Growth Factor-8 (rhFGF-8) remains stable up to 6 months at …
✓ Purity Verified by SDS-PAGE
✓ LAL Endotoxin-Tested

Functional Activity

ED50 < 5.0 ng/ml, measured by a cell proliferation assay using 3T3 cells in the presence of 1μg/ml of heparin, corresponding to a specific activity of > 2.0× 10ˆ5 units/mg.

Safety & Handling

This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.

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?

Reconstituted in ddH2O at 100 μg/ml. 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: ED50 < 5.0 ng/ml, measured by a cell proliferation assay using 3T3 cells in the presence of 1μg/ml of heparin, corresponding to a specific activity of > 2.0× 10ˆ5 units/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 < 0.2 EU/μg, 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?

Lyophilized recombinant human Fibroblast Growth Factor-8 (rhFGF-8) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-8 should be stable up to 2 weeks at 4°C or up 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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