| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Insulin-like growth factor I, Somatomedin C, IGF-1, IGFIA, IGF1, IBP1 |
| 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 rat IGF-I protein is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to IGF receptor 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: 7686.9 Da, Formula: C336H522N94O99S7.
- Source / origin: Recombinant, E. coli.
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys6-Cys48, Cys18-Cys61, and Cys47-Cys52
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
Insulin-like growth factor-I (IGF-I) belongs to the insulin family which is divided in two groups of peptides: 1- insulin and IGFs and 2- relaxin and insulin-like hormones. The structure of mature IGF-I is composed of a single polypeptide chain of 70 amino acids with 57 amino acids being identical across different organisms1,2.IGF-I is a pleiotropic factor responsible for the regulation of several cellular processes depending on its concentration, cell type and the developmental stage of the organisMIGF-I binds to IGF-I receptor and triggers the auto phosphorylation of the receptor and the activation of the insulin receptor substrates1.In the embryonic brain IGF-I expression is relatively high and drops sharply in the adult brain except in the hippocampus and the subventricular zone-olfactory bulb. In adults IGF-I is mainly synthesized in the liver though a process regulated by the growth hormone (GH). IGF-I can cross the blood-brain-barrier by binding to the IGF-I receptor present on endothelial cells and is later picked up by astrocytes to be transferred to neurons or directly by neurons1,2.Studies show that IGF-I influences neural stem cell proliferation and differentiation into neurons and glia as well as neuronal maturation including synapse formation. IGF-I also promotes adult neurogenesis by regulating neural stem cell number and differentiation1.
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.
Webb, R.L.
et al (1995) J. Cardiovasc. Pharmacol.26, S389.
Nieto-Estevez V.
et al. (2016) Front. Neurosci.10, 52.
