Growth Factors
Product List
FGF17 Mouse
Fibroblast Growth Factor 17 Mouse Recombinant
Fibroblast Growth Factor 17 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acid and having a molecular mass of approximately 22.5kDa.
FGF17 is purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile Filtered White lyophilized (freeze-dried) powder.
IGF1 E3R Human
Insulin Like Growth Factor-1, Mutant E3R Human Recombinant
IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa.
IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
IGF1 Gilthead Seabream
IGF1 Gilthead Seabream Recombinant
IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.
IGF-1 is purified by proprietary chromatographic techniques.
IGF1 Human
IGF-1 Human Recombinant
IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.
IGF-1 is purified by proprietary chromatographic techniques.
IGF1 Human Des1-3
Insulin-Like Growth Factor 1 Des (1-3) Human Recombinant
IGF-1 Des1-3 is purified by proprietary chromatographic techniques.
IGF1 Human, A67T
Insulin Like Growth Factor-1, Mutant A67T Human Recombinant
IGF1 A67T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa.
The IGF1 A67T is purified by proprietary chromatographic techniques.
IGF1 Human, A70T
Insulin Like Growth Factor-1, Mutant A70T Human Recombinant
IGF1 A70T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa.
The IGF1 A70T is purified by proprietary chromatographic techniques.
IGF1 Human, GST
Insulin-Like Growth Factor 1 Human Recombinant, GST Tag
IGF1 Human, R36Q
Insulin Like Growth Factor-1, Mutant R36Q Human Recombinant
IGF1 R36Q Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa.
The IGF1 R36Q is purified by proprietary chromatographic techniques.
IGF1 Human, V44M
Insulin Like Growth Factor-1, Mutant V44M Human Recombinant
IGF1 V44M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa.
The IGF1 V44M is purified by proprietary chromatographic techniques.
Introduction
Insulin-like growth factors (IGFs) are proteins with high sequence similarity to insulin. They are part of a complex system that cells use to communicate with their physiological environment. This system includes two main types of IGFs: IGF-1 and IGF-2. IGF-1 is primarily involved in growth and development, while IGF-2 is crucial for fetal development .
Key Biological Properties: IGFs are involved in cell proliferation, differentiation, and survival. They play a significant role in regulating normal physiology and various pathological states, including cancer .
Expression Patterns: IGF-1 is mainly secreted by the liver in response to growth hormone (GH) stimulation. IGF-2 is primarily involved in fetal development and is expressed in various tissues .
Tissue Distribution: IGFs are found in many tissues, including the liver, brain, and kidneys. They are also present in the blood, where they are bound to IGF-binding proteins (IGFBPs) that regulate their activity .
Primary Biological Functions: IGFs are essential for growth and development. IGF-1 promotes cell proliferation and inhibits apoptosis (cell death), while IGF-2 is crucial for early development .
Role in Immune Responses and Pathogen Recognition: IGFs have been shown to play roles in immune responses, although their exact mechanisms in pathogen recognition are still being studied .
Mechanisms with Other Molecules and Cells: IGFs exert their effects by binding to the IGF-1 receptor (IGF1R), which triggers a cascade of intracellular signaling pathways, including the MAPK and PI3K pathways .
Binding Partners: IGFs bind to IGF1R with high affinity. They can also bind to insulin receptors and IGF-2 receptors, although with lower affinity .
Downstream Signaling Cascades: Upon binding to IGF1R, IGFs activate several downstream signaling cascades that promote cell growth, survival, and differentiation .
Expression and Activity Control: The expression of IGFs is regulated by growth hormone (GH) and other factors such as nutrition, stress, and exercise .
Transcriptional Regulation: IGF genes are regulated at the transcriptional level by various transcription factors and hormones .
Post-Translational Modifications: IGFs undergo post-translational modifications, including phosphorylation and glycosylation, which affect their stability and activity .
Biomedical Research: IGFs are widely studied in biomedical research for their roles in growth, development, and disease .
Diagnostic Tools: IGF levels are measured as biomarkers for growth disorders and certain cancers .
Therapeutic Strategies: IGF analogs and inhibitors are being developed as potential therapies for growth deficiencies and cancer .
Development: IGFs are crucial for fetal development and growth during childhood .
Aging: IGF levels decline with age, which is associated with reduced muscle mass and increased risk of age-related diseases .
Disease: Dysregulation of IGF signaling is linked to various diseases, including cancer, diabetes, and neurodegenerative disorders .
