Description

IGF-1 LR3 1MG

We provide IGF-1 LR3 as a 1MG research growth-factor analog with a stated 99.1% purity. Furthermore, this long-arginine-3 form of insulin-like growth factor-1 contains a Glu-to-Arg substitution at position 3 together with an N-terminal 13-amino-acid extension. Consequently, researchers have investigated its receptor activity, cellular growth signaling, protein synthesis, and interactions with insulin-like growth factor-binding proteins.

IGF-1 LR3 Key Attributes

• Brand: AvigenLab
• Product: 1MG research presentation
• Quantity: 1MG
• Stated Purity: 99.1%
• Molecular Type: Modified Insulin-Like Growth Factor-1 Analog
• Structural Modification: Glu(3) → Arg(3)
• N-Terminal Modification: 13-Amino-Acid Extension
• Product Format: Vial
• Classification: Research Use Only
• Human Use: Not For Human Use

IGF-1 LR3 Product Overview

We provide IGF-1 LR3 for research involving growth-factor signaling, IGF-1 receptor biology, cellular proliferation, protein synthesis, and metabolic signaling. Moreover, published structural research shows that the modified molecule retains an overall IGF-I-like structure while incorporating substantial changes at the N-terminal region.

Additionally, experimental research demonstrates that the analog can activate the type 1 IGF receptor and insulin receptor in cultured cells. Therefore, researchers have used it to investigate receptor signaling and growth-factor responses under controlled experimental conditions.

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Product Identification

We identify IGF-1 LR3 as a long-arginine-3 analog of IGF-I carrying a defined structural modification at residue 3 and a 13-amino-acid N-terminal extension. Accordingly, its molecular architecture distinguishes it from native IGF-I and from shorter IGF-I analogs.

Product Category

We classify IGF-1 LR3 within our research growth-factor collection for studies involving receptor signaling, cellular growth, metabolism, and molecular biology. Moreover, its altered interaction with IGF-binding proteins has attracted particular research interest because binding-protein interactions can influence the biological availability of IGF-family molecules.

Scientific Characteristics

IGF-1 LR3 represents a modified IGF-I molecule incorporating a Glu(3)-to-Arg(3) substitution and a 13-residue N-terminal extension. Furthermore, structural investigations found that its core IGF-I domain maintains a highly similar overall structure while the major conformational differences occur around the modified N-terminal region.

Meanwhile, researchers have investigated its reduced binding to IGF-binding proteins as one factor contributing to its distinctive biological profile. Consequently, this characteristic makes the molecule useful for experimental studies examining relationships between ligand structure, binding-protein interactions, receptor activation, and cellular signaling.

Research Applications

We position IGF-1 LR3 for research involving IGF-1 receptor signaling, PI3K/Akt/mTOR pathways, MAPK signaling, cellular growth, protein synthesis, metabolic regulation, and growth-factor biology.

Additionally, IGF-1 receptor activation can engage IRS-1 and SHC adaptor proteins, subsequently connecting receptor activity with PI3K/Akt and Ras/MAPK signaling cascades. Therefore, researchers can examine downstream processes involving AKT, mTOR, FOXO, and related regulatory proteins within appropriate experimental systems.

Product Configuration

We provide IGF-1 LR3 in a 1MG vial carrying a stated 99.1% purity designation. Accordingly, the defined quantity, modified growth-factor identity, purity specification, vial presentation, and Research Use Only classification establish clear reference points for laboratory inventory.

Furthermore, this configuration allows researchers to distinguish the material from native IGF-I and other IGF-family research products through its specific product name, quantity, structural classification, and packaging format.

Product Features

The primary features include a 1MG quantity, 99.1% stated purity, modified IGF-I structure, and clearly defined research-use presentation. Additionally, the product label communicates Not For Human Use | Research Use Only.

Moreover, the scientific profile connects the molecule with IGF-1 receptor activation and downstream signaling pathways associated with cell growth and metabolism. Experimental research has also demonstrated enhanced receptor activation at lower concentrations compared with native IGF-I in specific cultured-cell systems. Nevertheless, such findings remain dependent on the experimental model and conditions.

Product Specifications

The structural modifications described above correspond with published characterization of Long-[Arg(3)]-IGF-I.

Intended Research Context

We identify the material as Research Use Only and Not For Human Use. Accordingly, our documentation focuses on laboratory investigation rather than therapeutic or consumer applications.

In particular, researchers can investigate the compound within experimental systems examining growth-factor receptors, cellular signaling, protein synthesis, metabolic pathways, and receptor-binding characteristics. Furthermore, published research has examined its activity in cultured mammalian cells and structural models.

Packaging Information

We present the product in a clearly labeled 1MG vial featuring our AvigenLab product presentation. The packaging communicates the 1MG quantity and stated 99.1% Purity designation while maintaining the Research Use Only classification.

Additionally, the vial format provides straightforward identification within our research catalog. Consequently, researchers can distinguish this presentation from other growth-factor and peptide configurations.

Regulatory Information

We classify the product as Research Use Only and maintain the Not For Human Use designation throughout our product documentation. Accordingly, scientific publications concerning Long-[Arg(3)]-IGF-I do not constitute regulatory approval for this specific AvigenLab presentation.

Moreover, experimental research establishes biological and structural characteristics without automatically establishing clinical applications. Therefore, we focus our documentation on molecular identity, research pathways, product specifications, and published scientific evidence rather than presenting experimental findings as established therapeutic outcomes.

Storage and Handling

We recommend following the storage and handling conditions specified in the applicable AvigenLab product documentation. Because protein and peptide stability can depend on formulation, packaging, environmental exposure, and other product-specific variables, we avoid assigning unsupported storage parameters.

Furthermore, researchers should maintain appropriate laboratory handling practices and follow the product-specific documentation associated with the material. Consequently, this approach supports consistent laboratory management without introducing assumptions about conditions that may vary between formulations.

Market Availability

Our presentation provides a defined 1MG research growth-factor configuration within our product collection. The product quantity, stated purity, modified IGF-I structure, vial format, and Research Use Only designation create clear reference points for laboratory inventory.

Moreover, Long-[Arg(3)]-IGF-I has a substantial research history spanning structural biology, receptor activation, cell culture, and growth-factor signaling. Likewise, studies have examined its interaction with IGF-binding proteins and its ability to activate IGF-related receptors under experimental conditions.

Product Reference

Our IGF-1 LR3 1MG presentation provides a defined modified IGF-I research material with a stated 99.1% purity designation. We document the material according to its structural modifications, receptor-signaling relevance, product configuration, research applications, and Research Use Only classification.

Consequently, the product provides researchers with a clearly identified material for investigating IGF-1 receptor activity, PI3K/Akt/mTOR signaling, MAPK pathways, cellular growth, metabolic regulation, and growth-factor biology. Furthermore, continued structural and cellular research provides additional insight into how modifications to the IGF-I molecule influence receptor activity and interactions with binding proteins.