IGF1 Rat

IGF-1 Rat Recombinant
Cat. No.
BT18481
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 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.
Shipped with Ice Packs
In Stock

Description

IGF-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa.
IGF-I is purified by proprietary chromatographic techniques.

Product Specs

Introduction

The insulin-like growth factors (IGFs), including IGF1 and IGF2, are peptides that have crucial roles in the growth and development of mammals. IGF1 is particularly important for mediating the effects of growth hormone (GH). Research has shown that GH doesn't directly promote sulfate incorporation into cartilage. Instead, it acts through a serum factor originally called 'sulfation factor' and later renamed 'somatomedin' (Daughaday et al., 1972). This discovery led to the identification of three main somatomedins: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

Description

Recombinant Rat IGF-1, produced in E. coli, is a single-chain polypeptide consisting of 70 amino acids. It is non-glycosylated and has a molecular weight of 7.7 kDa. The purification process of IGF-I involves proprietary chromatographic techniques.

Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein solution, at a concentration of 20mM in PBS with a pH of 7.0, was sterile-filtered through a 0.2µm filter before lyophilization.
Solubility
To reconstitute the lyophilized IGF1, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can then be further diluted as needed using other aqueous solutions.
Stability
Lyophilized IGF-1 remains stable at room temperature for up to 3 weeks; however, for long-term storage, it should be stored in a dry environment below -18°C. After reconstitution, IGF1 can be stored at 4°C for 2-7 days. For extended storage, it is recommended to store it below -18°C and add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
The purity of IGF-1 is determined using SDS-PAGE and is greater than 98.0%.
Biological Activity
The biological activity of IGF-1 is measured using a cell proliferation assay with FDC-P1 cells. The ED50, which is the concentration at which 50% of the maximum response is observed, is less than 2.0 ng/ml. This corresponds to a specific activity greater than 500,000 units/mg.
Synonyms
Somatomedin C, IGF-I, IGFIA, IGF1.
Source
Escherichia Coli.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.

Product Science Overview

Structure and Synthesis

IGF-1 is synthesized as a precursor protein that undergoes proteolytic processing to generate the mature form. In rats, IGF-1 is produced as four precursor isoforms with alternate N- and C-terminal propeptides . The mature IGF-1 protein consists of 70 amino acids and has a molecular mass of approximately 7.6 kDa . Recombinant IGF-1 is typically produced in Escherichia coli (E. coli) and purified using chromatographic techniques .

Biological Functions

IGF-1 is a key regulator of growth and development. It promotes cell proliferation and differentiation, particularly in muscle, bone, and cartilage tissues. IGF-1 also has significant effects on metabolism, including enhancing protein synthesis and glucose uptake. It plays a role in the regulation of apoptosis, thereby contributing to cell survival .

Expression Patterns and Tissue Distribution

IGF-1 is expressed in various tissues, with the highest levels found in the liver. It is also produced in other tissues, including muscle, bone, and cartilage, where it acts in an autocrine or paracrine manner. The expression of IGF-1 is regulated by several factors, including nutritional status, hormonal signals, and developmental stage .

Recombinant IGF-1 (Rat)

Recombinant rat IGF-1 is produced using recombinant DNA technology. The gene encoding rat IGF-1 is inserted into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed and purified. Recombinant IGF-1 is used in various research applications, including studies on cell growth, metabolism, and cancer .

Applications in Research

Recombinant IGF-1 is widely used in scientific research to study its effects on cell proliferation, differentiation, and survival. It is also used to investigate the mechanisms underlying growth and development, as well as its role in various diseases, including cancer and metabolic disorders. Additionally, IGF-1 is used in cell culture systems to promote the growth and maintenance of cells .

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