| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Heparin-Binding Growth Factor 2, Basic Fibroblast Growth Factor |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| 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 | |
| Target |
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.
(1994) Prog. Growth Factor Res. 5, 353.
Oda, Y.
et al. (2004) J. Oral Maxillofac. Surg. 62, 73.
Yetgin, S.
et al. (2001) Leuk. Lymphoma 42, 83.
Strutz, F.
et al. (2002) Kidney Int. 61, 1714.
Slavin, J.
(1995) Cell Biol. Int. 19, 431.
Bikfalvi, A.
et al. (1997) Angiogenesis 1, 155.
Bruno, E.
et al. (1991) Blood77, 2339.
Huang, S. and Terstappen, L.W.
(1992) Nature 360, 745.
Bansal, R. and Pfeiffer, S.E.
(1997) J. Neurosci. Res. 50, 215.
Halaban, R.
(1996) Semin. Oncol. 23, 673.
Florkiewicz, R.Z. and Sommer. A.
(1989) Proc. Nat. Acad. Sci. U.S.A. 86, 3978.
Allouche, M.
(1995) Leukemia 9, 937.
Mignatti, P.
et al. (1992) J. Cell Physiol. 151, 81.
Jaye, M.
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.
et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 3012.
Grinspan, J.B.
et al. (1993) J. Neurosci. Res. 36, 672.
Grinspan, J.B.
et al. (1993) J. Neurosci. Res. 36, 672.