IGF-I (30-41) (TFA) is amino acids 30 to 41 fragment of Insulin-like Growth Factor I (IGF-I). IGF-I is partly responsible for systemic GH activities although it possesses a wide number of own properties (anabolic, antioxidant, anti-inflammatory and cytoprotective actions).
IGF-I (30-41) TFA is a synthetic peptide fragment derived from the C-domain of human insulin-like growth factor I, encompassing amino acids 30 to 41. As a truncated segment of IGF-I, this compound preserves a region implicated in receptor binding and downstream signaling modulation, making it a valuable tool for dissecting the molecular mechanisms of IGF-mediated pathways. The TFA designation indicates the trifluoroacetate salt form, commonly used to enhance peptide solubility and handling in laboratory settings. Researchers utilize this peptide to investigate specific sequence motifs within the IGF-I structure, particularly their roles in cellular communication, metabolic regulation, and growth factor signaling. Its well-defined sequence and manageable size allow for targeted biochemical studies, positioning it as a versatile reagent in peptide-based research.
Receptor interaction analysis: IGF-I (30-41) TFA serves as a strategic probe for exploring the interactions between IGF-I and its cognate receptors, including IGF-IR and hybrid insulin/IGF receptors. By isolating the C-domain fragment, investigators can assess the contribution of this specific region to receptor binding affinity and specificity. Such studies are instrumental in mapping critical contact points within the ligand-receptor interface, providing insights into the structural determinants of IGF-I signaling. This information is essential for understanding how modifications within the C-domain may alter receptor activation and subsequent cellular responses.
Signal transduction research: The peptide fragment enables detailed examination of downstream signaling cascades triggered by IGF-I receptor engagement. Because the 30-41 region is implicated in modulating receptor conformation and activation, using this peptide allows researchers to dissect the sequence-dependent effects on pathways such as PI3K/Akt and MAPK/ERK. By introducing the fragment into cell-based assays or in vitro signaling models, it becomes possible to delineate the specific contributions of the C-domain to the broader IGF-I signaling network, facilitating the identification of novel regulatory nodes.
Peptide structure-function studies: IGF-I (30-41) TFA is frequently employed in structure-activity relationship (SAR) analyses to evaluate how alterations within the C-domain affect the biological activity of IGF-I and its analogs. Synthetic modification of this sequence, combined with comparative functional assays, allows researchers to pinpoint key residues responsible for receptor interaction, stability, and signaling potency. These studies support the rational design of peptide mimetics or antagonists with tailored properties, advancing both basic and applied peptide science.
Peptide synthesis validation: As a well-characterized peptide fragment, IGF-I (30-41) TFA is used as a reference standard or positive control in peptide synthesis workflows. Its defined sequence and established analytical profiles make it suitable for calibrating chromatographic, mass spectrometric, and spectroscopic techniques. Utilizing this fragment in validation procedures ensures the reliability and reproducibility of synthetic protocols, which is critical for laboratories engaged in custom peptide production or quality control.
Biochemical assay development: The C-domain fragment finds application in the development and optimization of biochemical assays aimed at quantifying IGF-related activity or screening for modulators of IGF-I function. Its manageable size and specificity facilitate incorporation into binding assays, competitive inhibition formats, and biosensor platforms. Employing this peptide in assay development supports the creation of robust, sensitive, and selective tools for investigating IGF-I biology, screening compound libraries, or monitoring biomolecular interactions relevant to growth factor research.
2. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
5. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More