IGF1 Mouse

Insulin-Like Growth Factor 1 Mouse Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT18175
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IGF1 N15 Human

Insulin Like Growth Factor-1 N15 Labeled Human Recombinant

IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled.

The IGF1 N15 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18271
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IGF1 Rabbit

Insulin-Like Growth Factor 1 Rabbit Recombinant

Insulin-Like Growth Factor-I Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 7639 Dalton. 
Shipped with Ice Packs
Cat. No.
BT18408
Source
Escherichia Coli. 
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IGF1 Rat

IGF-1 Rat Recombinant

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.

Shipped with Ice Packs
Cat. No.
BT18481
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IGF2 Human

IGF-2 Human Recombinant

Insulin-Like Growth Factor- II Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids and having a molecular mass of 7.5k Dalton.                  

IGF-II is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18538
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IGF2 Mouse

Insulin Like Growth Factor-2 Mouse Recombinant

IGF2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, monomeric polypeptide chain containing 67 amino acids and having a total molecular mass of 7.4kDa.
The IGF2 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18615
Source

Escherichia Coli.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IGFBP4 Sf9, Human

Insulin Like Growth Factor Binding Protein-4 Human Recombinant, Sf9

Insulin Like Growth Factor Binding Protein-4 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 237 amino acids and having a molecular mass of 30kDa. The IGFBP4 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18674
Source

Sf9, Insect cells.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

LR3 IGF1 Human

LR3 Insulin Like Growth Factor-1 Human Recombinant

The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals.
Recombinant Human LR3 Insulin Like Growth Factor-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9.1kDa.
Shipped with Ice Packs
Cat. No.
BT18739
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

pro-IGF2 Human

Pro-Insulin Like Growth Factor-2 Human Recombinant

Pro-IGF2 Human Recombinant produced in HEK cells is a glycosylated monomer, contains 157 a.a. (24-180) having a total molecular weight of 25kDa.
The Pro-IGF2 contains a C-terminal propeptide (E peptide) Arg92 to Lys180 and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18848
Source
HEK.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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