The IGFs are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar by structure and function to insulin, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions.
The predicted molecular weight of Recombinant Mouse IGF-I is Mr 7.6 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is 8 kDa (reducing conditions).
Predicted Molecular Mass
7.6
Formulation
This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
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Recombinant Mouse IGF-I is widely used in research because it is a potent growth factor that regulates cell proliferation, survival, differentiation, and migration, making it essential for studies involving muscle growth, tissue repair, cancer biology, and metabolic regulation.
Key scientific applications and advantages include:
Muscle Regeneration and Repair: IGF-I is a critical factor for muscle growth and repair. It increases muscle mass and strength, reduces degeneration, and inhibits excessive inflammation in skeletal muscle injury models. Recombinant Mouse IGF-I has been shown to improve functional recovery in models of muscular dystrophy and other neuromuscular disorders.
Cell Proliferation and Survival: IGF-I stimulates cell proliferation in various cell types, including myeloid cells, endothelial cells, and cancer cell lines. It promotes cell survival and differentiation, which is valuable for cell culture, organoid development, and tissue engineering studies.
Cancer and Tumor Biology: Many neoplastic cells produce IGF-I, which regulates energy metabolism, proliferation, and cell survival. Recombinant IGF-I is used to study tumor progression, cancer stem cell interactions, and the effects of IGF-I signaling on cancer-associated fibroblasts.
Fibrosis and Tissue Remodeling: IGF-I has demonstrated antifibrotic effects in liver fibrosis models, enhancing tissue regeneration and reducing collagen deposition. Recombinant IGF-I can be used to investigate mechanisms of fibrosis and potential therapeutic interventions.
Bone Formation and Regeneration: IGF-I directly enhances bone density and regeneration, making it useful for studies on bone biology and repair, especially in aged or osteoporotic models.
Immunology and Hematopoiesis: IGF-I, in combination with cytokines like IL-3, stimulates differentiation and proliferation of myeloid cells and regulates lymphopoiesis, supporting research in hematopoietic and immune cell development.
Standardization and Reproducibility: Recombinant proteins offer high purity, batch-to-batch consistency, and defined activity, which are critical for reproducible experimental results and quantitative assays.
In summary, Recombinant Mouse IGF-I is a versatile tool for research in cell biology, regenerative medicine, cancer, immunology, and metabolic studies due to its well-characterized biological activities and broad relevance across multiple physiological and pathological processes.
Yes, recombinant mouse IGF-I can be used as a standard for quantification or calibration in ELISA assays, provided it is appropriately validated and matched to your assay system. This is a common practice in research ELISAs for IGF-I, as most commercial kits use recombinant IGF-I as their standard.
Key considerations and supporting details:
Recombinant IGF-I as Standard: Most mouse IGF-I ELISA kits use recombinant IGF-I, typically expressed in E. coli, as the standard for generating the calibration curve. These standards are designed to be recognized by the assay antibodies and to mimic the behavior of endogenous IGF-I in the assay system.
Validation and Parallelism: It is important to confirm that the recombinant IGF-I standard produces a standard curve that is parallel to the response obtained from endogenous IGF-I in your sample matrix (e.g., serum, plasma, cell culture supernatant). Parallelism ensures that the quantification is accurate for both recombinant and natural forms.
Amino Acid Sequence and Modifications: Ensure that the recombinant IGF-I you use matches the mature, biologically active form of mouse IGF-I (typically a 70-amino acid peptide). Some standards may use truncated or modified forms, which could affect antibody recognition and quantification.
Matrix Effects: Prepare your standard curve in the same diluent or matrix as your samples to minimize matrix effects and ensure accurate quantification. For example, if your samples are serum, dilute the recombinant standard in serum or a suitable serum diluent.
Research Use Only: Recombinant IGF-I standards and the resulting quantification are for research use only and not for diagnostic purposes.
Controls: Include appropriate controls, such as endogenous positive controls, to validate the performance of your standard and assay.
Protocol Recommendations:
Reconstitute and dilute the recombinant IGF-I according to your ELISA kit instructions or validated laboratory protocol.
Generate a standard curve covering the expected concentration range of your samples (e.g., 31.3–2000 pg/mL).
Confirm that the standard curve is linear and that sample dilutions fall within the linear range.
Summary Table: Use of Recombinant Mouse IGF-I as ELISA Standard
Requirement
Recommendation/Note
Protein form
Full-length, mature mouse IGF-I (70 aa)
Expression system
Typically E. coli; ensure compatibility with assay antibodies
Validation
Confirm parallelism with endogenous IGF-I in your sample matrix
Matrix for standard curve
Match to sample matrix (e.g., serum, plasma, culture medium)
Application
Research use only
Controls
Include endogenous positive controls
In summary: Recombinant mouse IGF-I is widely accepted and validated as a standard for ELISA quantification, provided it is matched to the assay and validated for parallelism with endogenous IGF-I in your samples.
Recombinant Mouse IGF-I has been validated for a broad range of applications in published research, including functional assays, cell proliferation assays, ELISA, Western blot, immunohistochemistry, blocking assays, in vivo studies, and cell culture.
Key validated applications include:
Functional Assays: Used to assess biological activity, such as stimulation of cell proliferation (e.g., MCF-7 cell line).
Cell Proliferation and Bioassays: Demonstrated to stimulate cell proliferation in serum-free conditions and used in various bioassays to study cellular responses.
ELISA: Employed as a standard or analyte in enzyme-linked immunosorbent assays to quantify IGF-I levels.
Western Blot: Validated for detection and quantification of IGF-I protein in samples.
Immunohistochemistry: Used to localize IGF-I in tissue sections.
Blocking Assays: Applied to block IGF-I activity in functional studies.
In Vivo Assays: Used in animal models to study physiological effects, such as muscle regeneration, radioprotection, and tumor growth modulation.
Cell Culture: Supplemented in culture media to support growth and differentiation of various cell types, including organoids and stem/progenitor cells.
Representative published research applications:
Muscle Regeneration: Local administration of IGF-I (including mRNA and recombinant protein) accelerates muscle regeneration in mouse models of injury.
Neurobiology: Promotes axonal regrowth in retinal injury models and modulates neurogenesis and oligodendrogenesis from adult stem/progenitor cells.
Cancer Biology: Modulates tumor cell growth, invasion, and radioprotection in cancer models.
Immunology: Influences macrophage function and immune responses, including antimicrobial mechanisms and pro-regenerative macrophage recruitment.
Metabolic and Endocrine Research: Studied for its role in glucose transport, bone formation, and endocrine signaling.
These applications are supported by peer-reviewed studies and product validation data, confirming the utility of recombinant Mouse IGF-I in diverse experimental systems.
To reconstitute and prepare Recombinant Mouse IGF-I protein for cell culture experiments, dissolve the lyophilized protein in sterile water or PBS to a concentration of 0.1–1.0 mg/mL, avoiding vigorous mixing such as vortexing. For optimal stability and activity, follow these steps:
Centrifuge the vial briefly before opening to ensure all material is at the bottom.
Add sterile water or PBS directly to the vial to achieve your desired stock concentration (commonly 0.1–1.0 mg/mL).
Gently mix by pipetting up and down or swirling; do not vortex, as this may denature the protein.
If the protein forms a film, ensure it is fully dissolved by gentle mixing.
For short-term storage (up to 1 week), keep the reconstituted protein at 2–8°C.
For long-term storage, aliquot the solution and store at –20°C to –80°C, ideally in a buffer containing a carrier protein such as 0.1% BSA to prevent adsorption and loss of activity.
Avoid repeated freeze-thaw cycles to maintain protein integrity.
Preparation for cell culture:
Before adding to cell cultures, dilute the stock solution to the desired working concentration using sterile cell culture medium or buffer.
Typical working concentrations for IGF-I in cell culture range from 0.1 to 100 ng/mL, depending on the cell type and experimental design.
If using for functional assays, do not add preservatives such as sodium azide.
Summary of best practices:
Use sterile technique throughout.
Prepare aliquots to avoid repeated freeze-thaw.
Include carrier protein (e.g., BSA) for long-term storage.
Do not vortex or subject to harsh agitation.
These steps will help ensure the recombinant IGF-I retains its biological activity and is suitable for cell culture applications.
Products are for research use only. Not for use in diagnostic or therapeutic procedures.
