IGF1 Mouse

Insulin-Like Growth Factor 1 Mouse Recombinant
Cat. No.
BT18175
Source
Escherichia Coli.
Synonyms
Somatomedin C, IGF-I, IGFIA, IGF1.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Insulin-Like Growth Factor I mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7600 Dalton.
IGF-I is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The insulin-like growth factors (IGFs), also known as somatomedins, are a family of peptides that play crucial roles in mammalian growth and development. IGF1 is a key mediator of growth hormone's (GH; MIM 139250) growth-promoting effects. Initial research revealed that growth hormone's impact on sulfate incorporation into cartilage was not direct but rather mediated through a serum factor called 'sulfation factor,' which was later renamed 'somatomedin' (Daughaday et al., 1972). Three primary somatomedins have been identified: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Description
Recombinant Mouse Insulin-Like Growth Factor I, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 70 amino acids with a molecular weight of 7.6 kDa. The purification of IGF-I is achieved using proprietary chromatographic methods.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized without any additional ingredients.
Solubility
For reconstitution of the lyophilized IGF1, it is recommended to use sterile 18MΩ-cm H2O at a concentration not less than 100 µg/ml. Further dilutions can be made using other aqueous solutions.
Stability
Lyophilized IGFI, while stable at room temperature for up to 3 weeks, should be stored in a dry environment below -18°C. After reconstitution, IGF-1 should be stored at 4°C for 2-7 days. For long-term storage, it is recommended to store below -18°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined by two methods: (a) RP-HPLC analysis and (b) SDS-PAGE analysis. The purity is greater than 98.0%.
Biological Activity
The ED50, determined by the dose-dependent proliferation of murine BALB/C 3T3 cells (measured by 3H-thymidine uptake), is less than 1.0 ng/ml. This corresponds to a specific activity of 1MU/mg.
Protein Content
Protein quantification is performed using two independent methods: 1. UV spectroscopy at 280 nm, using an absorbance value of 0.47 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF-I as a reference standard.
Synonyms
Somatomedin C, IGF-I, IGFIA, IGF1.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Glu-Thr-Leu.

Product Science Overview

Structure and Synthesis

IGF-1 is synthesized as two precursor isoforms with alternate N- and C-terminal propeptides . These isoforms are differentially expressed by various tissues, indicating the versatility of IGF-1 in different biological contexts . The protein consists of 70 amino acids in a single chain with three intramolecular disulfide bridges, giving it a molecular weight of approximately 7,649 daltons .

Biological Properties and Functions

IGF-1 is a key mediator of anabolic activities in numerous tissues and cells. It contributes to growth hormone-stimulated growth, metabolism, and protein translation . The highest rates of IGF-1 production occur during the pubertal growth spurt, while the lowest levels are observed in infancy and old age . IGF-1 is essential for the maintenance of muscle strength, muscle mass, and the development of the skeleton. It also plays a significant role in brain, eye, and lung development during fetal development .

Modes of Action

IGF-1 exerts its effects by binding to the IGF-1 receptor (IGF1R), which is predominantly expressed by neurons . This binding activates intracellular signaling pathways that promote cell growth, differentiation, and survival. IGF-1 also has neuroprotective properties, protecting neurons from cytokine-induced death .

Regulatory Mechanisms

The production of IGF-1 is regulated by pituitary growth hormone (GH) . Most of IGF-1 is bound to one of six binding proteins (IGF-BP), which modulate its activity and availability . IGFBP-1, for instance, is regulated by insulin . Additionally, proinflammatory mediators such as lipopolysaccharide (LPS), poly (I:C), and IFNγ can suppress IGF-1 production, while cAMP analogs can increase its production .

Recombinant Mouse IGF-1

Recombinant mouse IGF-1 is a laboratory-produced version of the naturally occurring protein. It is used in various research applications to study its effects on growth, development, and cellular metabolism. The recombinant form allows scientists to investigate the specific roles and mechanisms of IGF-1 in a controlled environment, providing valuable insights into its biological functions and potential therapeutic applications .

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