Recombinant human FGF-b protein

SKU:BHP21300042 Toxins and Venom Peptides
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Alomone Labs
Alomone Labs
Details Products
Overview
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Recombinant human FGF-b protein is a reagent targeting FGF. Key specifications include Form: Lyophilized; Purity: ≥98% (HPLC); MW: 16.5 kDa. Commonly used in neuroscience studies, including measure fgf modulation in patch-clamp electrophysiology (dose–response) and profile fgf pharmacology in cell-based assays (concentration–response + time-course).
Target FGF
Purity ≥98% (HPLC)
Molecular Weight 16.5 kDa
Form Lyophilized
Available Options

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

  • Options:
    Size (7) - 0.1 ml, 0.25 mg, 0.5 mg, 1 mg, 10 mcg, 25 mcg, 50 mcg
    Quantity: 1
  • Lead time: typically ships in ~1-2 business days; timing may vary by selected option.
  • Storage: Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Storage after reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. Storage of solutions: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No F-170
Accession Number P09038
Activity
  • FGF-basic is a heparin binding growth factor which stimulates the proliferation of a wide variety of cells
  • including mesenchymal
  • neuroectodermal
  • endothelial
  • and smooth muscle cells
  • among many others. FGF-basic also induces neuronal and glial differentiation
  • survival and regeneration1-4.
Alternative Names Heparin-Binding Growth Factor 2, Basic Fibroblast Growth Factor
Concentration EC50 = ~17 pM
Form Lyophilized
Formulation Lyophilized from filtrated Ammonium acetate solution. May contain acetate as a residual counter ion.
Gene ID FGF2, FGFR1, FGFR2, FGFR3, FGFR4, CSPG4, FGFBP1, TEC, FGFBP3, ITGAV, ITGB3
Molecular Weight 16.5 kDa
Product Type
  • Proteins & Peptides
  • Proteins
Purity ≥98% (HPLC)
Reconstitution Centrifuge the vial (10,000 × g for 5 minutes) before adding solvent to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Gently tap, tilt, and roll the vial to aid dissolution. Avoid vigorous vortexing; light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. For long-term storage of diluted solutions, we recommend adding 0.1% BSA. Repeated freeze-thaw cycles may result in loss of activity.
Solubility Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. For long-term storage of diluted solutions, we recommend adding 0.1% BSA. Repeat freeze-thawing may result in loss of activity.
Source Recombinant, E. coli
Storage Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Storage after reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. Storage of solutions: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.
Target FGF receptors

Overview

Recombinant human FGF-b protein is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to FGF receptors biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Cell proliferation assay.

Key elements and design rationale

  • Molecular identity: MW: 16.5 kDa.
  • Source / origin: Recombinant, E. coli.
  • Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: Yes.

When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.

Biological background

Fibroblast growth factor-basic (FGF-b, FGF-2) belongs to the 23 member FGF family.1 FGFs play major roles in development,2 wound healing,3 hematopoiesis,4 tumorigenesis,5 and angiogenesis.6 It is expressed mostly in tissues of mesoderm and neuroectoderm origin.7FGF-basic exists in four molecular forms, three high molecular weight (21.5, 22, and 24 kDa), and one 18 kDa forM8 The higher molecular weight forms are mainly nucleus associated. The 18 kDa form, which lacks a signal sequence, is cytoplasmic or found at the cell surface.9FGF-basic may be released from damaged cells or could be released by an exocytotic mechanism that is independent of the ER-Golgi pathway.10 Secreted FGF interacts with specific cell surface receptors. The FGF receptor family consists of four members: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. These receptors comprise a conserved tyrosine kinase domain, a transmembrane domain and an extracellular ligand binding domain.11 Binding of FGF-basic to its receptor is regulated by heparan sulfate proteoglycans.12FGF-basic is implicated in many biological processes. It has been shown to induce endothelial cell proliferation, migration and angiogenesis in vitro and in vivo,13 stimulate myeloid progenitors,14 stimulate stromal growth,15 promote the release of endothelium from its connective tissue anchor (thus encouraging the entry of new vascular endothelium),6 regulate oligodendrocyte progenitor proliferation and differentiation in culture,16 and play a role in the autonomous growth of melanoma cells.17

Research relevance and current trends

  • Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
  • Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
  • Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.

Common research applications

  • Cell proliferation assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.

Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.

Notes for experimental interpretation

  • Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
  • Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
  • Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
  • Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Behrendt, H.J.

et al. (2004) Br. J. Pharmacol.141, 737.

Fernig, D.G. and Gallagher, J.T.

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Bansal, R. and Pfeiffer, S.E.

(1997) J. Neurosci. Res. 50, 215.

Halaban, R.

(1996) Semin. Oncol. 23, 673.

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(1989) Proc. Nat. Acad. Sci. U.S.A. 86, 3978.

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et al. (1992) J. Cell Physiol. 151, 81.

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et al. (1992) Biochim. Biophys. Acta. 1135, 185.

Ornitz, D.M.

(2000) BioEssays 22, 108.

Bikfalvi, A.

et al. (1997) Endocr. Rev. 18, 26.

Bikfalvi, A.

et al. (1997) Endocr. Rev. 18, 26.

Ornitz, D.M. and Itoh, N.

(2001) Genome Biol. 2, 3005.1.

Morrison, R.S.

et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7537.

Walicke, P.

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