Recombinant Mouse FGF-Basic

Recombinant Mouse FGF-Basic (FGF-2) is a highly valuable tool for a wide range of research applications due to its critical roles in regulating fundamental cellular processes. Here are several key reasons why you should consider using Recombinant Mouse FGF-Basic in your research:

1. Supports Stem Cell Culture and Maintenance

• Recombinant Mouse FGF-Basic is essential for maintaining human and mouse embryonic stem cells in an undifferentiated state in culture systems. It helps preserve pluripotency and supports long-term expansion of stem cells, making it indispensable for stem cell research and regenerative medicine studies.

2. Promotes Cell Proliferation and Survival

• FGF-Basic stimulates the proliferation and survival of various cell types, including fibroblasts, endothelial cells, and neural stem cells. This makes it useful for experiments requiring robust cell growth, such as in tissue engineering, wound healing models, and developmental biology.

3. Enhances Angiogenesis and Tissue Repair

• FGF-Basic is a potent angiogenic factor, promoting the formation of new blood vessels. It is widely used in studies of wound healing, tissue regeneration, and vascular biology, where it accelerates repair processes and improves outcomes in experimental models.

4. Regulates Differentiation and Development

• FGF-Basic plays a crucial role in embryonic development, differentiation, and organogenesis. It is involved in the regulation of neuronal function, bone formation, and cartilage homeostasis, making it relevant for developmental biology and disease modeling.

5. Facilitates Disease Modeling and Therapeutic Research

• FGF-Basic has been studied in models of neurodegeneration, cardiovascular disease, and cancer. Its ability to modulate cell survival, differentiation, and tissue repair makes it a key molecule for investigating disease mechanisms and developing potential therapies.

6. High Quality and Consistency

• Recombinant Mouse FGF-Basic is produced using advanced biotechnological methods, ensuring high purity, activity, and batch-to-batch consistency. This reliability is crucial for reproducible experimental results and regulatory compliance in research.

7. Versatile Applications

• The protein can be used in a variety of applications, including cell culture, bioassays, ELISA standards, and Western blot controls. Its versatility makes it suitable for both basic research and translational studies.

8. Well-Characterized and Widely Used

• Recombinant Mouse FGF-Basic is well-characterized and has been extensively used in published research, providing a solid foundation for your experiments and facilitating comparison with existing literature.

In summary, Recombinant Mouse FGF-Basic is a powerful and versatile tool that supports a broad spectrum of research applications, from stem cell biology and tissue engineering to disease modeling and therapeutic development. Its ability to regulate key cellular processes makes it an essential component for advancing scientific understanding and innovation.

Yes, recombinant mouse FGF-basic can be used as a standard for quantification or calibration in ELISA assays, provided it is compatible with your assay system. Multiple sources confirm that recombinant mouse FGF-basic is suitable as an ELISA standard, and commercial ELISA kits often use recombinant FGF-basic as their calibration standard.

Key considerations and supporting details:

• Assay Compatibility: Ensure that the recombinant FGF-basic you use matches the species and isoform recognized by your ELISA antibodies. Most mouse FGF-basic ELISA kits are validated to detect both natural and recombinant forms, and their standard curves are generated using recombinant FGF-basic.
• Source and Expression System: Recombinant FGF-basic is commonly produced in E. coli or yeast. While both are suitable for ELISA standards, minor differences in folding or post-translational modifications can affect antibody recognition in rare cases. However, most commercial kits report parallel dose-response curves for recombinant and natural FGF-basic, indicating functional equivalence for quantification.
• Standard Preparation: Follow best practices for reconstitution and dilution of the recombinant standard, as outlined in your ELISA kit protocol. Use freshly prepared standards for each assay to ensure accuracy.
• Validation: If you are developing a custom ELISA, validate that your recombinant standard produces a standard curve parallel to that of endogenous FGF-basic in your sample matrix. This ensures accurate quantification.

Limitations:

• The recombinant standard should be of high purity and free from carrier proteins or preservatives that could interfere with the assay.
• For absolute quantification, ensure the protein concentration of your recombinant standard is accurately determined.

Summary Table: Use of Recombinant Mouse FGF-Basic as ELISA Standard

In conclusion, recombinant mouse FGF-basic is appropriate for use as a standard in ELISA quantification and calibration, provided it is validated for your specific assay system and sample type.

Research Applications of Recombinant Mouse FGF-Basic

Recombinant mouse FGF-basic (FGF-2) has been validated across a diverse range of research applications in published literature, spanning developmental biology, regenerative medicine, and disease modeling.

Cell Culture and Stem Cell Maintenance

FGF-basic serves as a critical component in human embryonic stem cell culture systems, where it is necessary for maintaining pluripotency and preventing differentiation. The protein is routinely used in serum-free culture media formulations designed for stem cell expansion and maintenance. Additionally, it has been applied in 3D culturing protocols for human pluripotent stem cell-derived endothelial cells intended for vascular regeneration applications.

Developmental and Differentiation Studies

The protein has been validated in research examining embryonic development and differentiation processes. Studies have utilized recombinant mouse FGF-basic in investigations of pluripotency factor regulation and Hox cluster activation in early embryos. It has also been employed in research on neocortical neurogenesis, including studies examining how maternal hyperglycemia affects neural development.

Tissue Regeneration and Repair

FGF-basic has demonstrated utility in research focused on direct cellular reprogramming and tissue regeneration. Studies have employed the protein in protocols for extracellular vesicle-guided direct reprogramming of fibroblasts into functional cardiomyocytes. Research on perivascular adipose-derived stem cell differentiation toward smooth muscle cells has also incorporated FGF-basic signaling pathways.

Neurological Research

The protein has been validated in neural stem cell research, including studies investigating small extracellular vesicle-based delivery systems for reducing apoptosis and neuroinflammation following traumatic spinal cord injury. These applications leverage FGF-basic's role in neuronal function and survival pathways.

Standard Laboratory Applications

Beyond specialized research, recombinant mouse FGF-basic has been validated for use as an ELISA standard, Western blot control, and in cell proliferation bioassays. The protein's bioactivity has been characterized through NR6R-3T3 mouse fibroblast cell proliferation assays, with typical ED₅₀ values of 2.5 ng/mL or less.

To reconstitute and prepare Recombinant Mouse FGF-Basic (FGF2/bFGF) protein for cell culture experiments, dissolve the lyophilized protein in sterile buffer at a recommended concentration of 100 μg/mL (0.1 mg/mL), using either sterile water or sterile PBS, ideally containing at least 0.1% carrier protein such as bovine serum albumin (BSA).

Step-by-step protocol:

• Before opening the vial: Briefly centrifuge the lyophilized protein vial (20–30 seconds in a microcentrifuge) to collect all powder at the bottom.
• Warm to room temperature: Allow the vial to equilibrate to room temperature before opening to minimize condensation.
• Reconstitution buffer: Use sterile distilled water or sterile PBS. For optimal stability and recovery, include 0.1% BSA as a carrier protein in the buffer.
• Concentration: Add buffer to achieve a final concentration of 0.1–1.0 mg/mL (e.g., for 100 μg protein, add 1 mL for 0.1 mg/mL or 100 μL for 1 mg/mL).
• Gentle mixing: Do not vortex. Gently mix by pipetting or slow inversion. Allow several minutes for complete dissolution; if solubility issues arise, incubate at 4 °C overnight.
• Aliquoting: Divide into small working aliquots to avoid repeated freeze-thaw cycles.
• Storage: Store aliquots at –20 °C to –80 °C. Avoid repeated freeze-thaw cycles, which can denature the protein.
• Sterilization: If needed, filter-sterilize diluted working solutions using a low-protein-binding 0.22 μm filter.
• Dilution for cell culture: Further dilute the stock solution in cell culture medium immediately before use. Final working concentrations for cell culture typically range from 0.3–10 ng/mL, depending on cell type and experimental requirements.

Additional notes:

• Carrier protein (BSA or serum albumin) helps stabilize FGF-Basic and prevents adsorption to tube walls, especially at low concentrations.
• Avoid vigorous mixing or vortexing, which may denature the protein.
• Confirm protein recovery by SDS-PAGE if needed.
• Always consult the specific product datasheet for buffer recommendations, as some formulations may require specific pH or additives.

Summary Table:

This protocol ensures optimal solubility, stability, and biological activity of recombinant mouse FGF-Basic for cell culture applications.