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Your Position: Home > Insulin-like Growth Factor（IGF）Family

Insulin-like Growth Factor（IGF） Family

Insulin-like Growth Factor（IGF） Family
INTRODUCTION
PRODUCT LIST
VERIFICATION DATA
REFERENCES
Introduction

Insulin-like growth factor (IGF) is a group of growth hormones that play a key role in regulating the signaling processes critical to cell proliferation, differentiation, and survival. These growth factors are expressed in various tissues and cell types, with autocrine, paracrine and endocrine functions. There are two types of IGFs, type I(IGF-I) and type II (IGF-II), act by binding to their specific membrane receptors: IGF-I R and IGF-II R.

As with IGF, IGF receptors are also potential targets for targeted therapies. IGF-I R is a heterotetrameric transmembrane protein with two disulfide-linked alpha subunits and two transmembrane beta subunits. Activation of this pathway has been linked to cancer initiation and growth, with many types of tumor cells overexpressing IGF-IR to promote resistance to radiotherapy, chemotherapy and targeted therapies. To overcome this resistance, IGF / IGF-IR targeted therapies have become a viable cancer treatment strategy. Teprotumumab, a representative drug targeting IGF-IR, was approved by the US Food and Drug Administration (FDA) in 2020 for the treatment of thyroid-associated ophthalmopathy (TAO). Initial studies suggest that combined targeting of IGF-IR and STAT3 may inhibit tumor metastasis and overcome resistance to STAT3-mediated anti-IGF-IR therapy, maximizing the efficacy of cancer treatment.

Schematic diagram of IGF-targeted drugs

Schematic diagram of IGF-targeted drugs

https://doi.org/10.1016/j.gendis.2022.03.002
Therapeutic strategies to inhibit IGF-IR signaling

Therapeutic strategies to inhibit IGF-IR signaling

https://doi.org/10.3390/ijms231911781

ACROBiosystems has developed a series of HEK293-expressed IGF and IGF receptor family proteins, including IGF-IR tetrameric protein, IGF-I, IGF-II, IGFBP-3, IGFBP-4 and IGFBP-7. The IGF family proteins are available in various species and tags, with high purity and high structural homogeneity verified by SDS-PAGE/SEC-MALS. High bioactivity was also validated by ELISA/SPR. Our proteins also undergo a strict quality control system to ensure stable performance in immunization, antibody drug screening and characterization studies to help drug development targeting IGF.

PRODUCT LIST
Molecule Cat. No. Species Product Description Preorder/Order
Verification Data
High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS
IGR-H5229

The purity of Human IGF-I R, His Tag (Cat. No. IGR-H5229) is more than 90% and the molecular weight of this protein is around 252-308 kDa verified by SEC-MALS.

High biological activity verified by ELISA

IGR-H5229

Immobilized Human IGF-I R, His Tag (Cat. No. IGR-H5229) at 5 μg/mL (100 μL/well) can bind Human IGF-I, Fc Tag (Cat. No. IG1-H4269) with a linear range of 0.01-0.625 μg/mL (QC tested).

IGR-H5229

Immobilized Human IGF-I R, His Tag (Cat. No. IGR-H5229) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IGF-I, Avitag,Fc Tag (Cat. No. IG1-H82F7) with a linear range of 0.02-0.625 μg/mL (QC tested).

High biological activity verified by SPR

IL1-H82E8

Human IGFBP-7, His Tag (Cat. No. IG7-H5240) immobilized on CM5 Chip can bind Human C1q R1, His Tag (Cat. No. C11-H5228) with an affinity constant of 16.7 μM as determined in a SPR assay (Biacore 8K) (Routinely tested).

IL3-H82E5

Human IGF-I R, His Tag (Cat. No. IGR-H5229) immobilized on CM5 Chip can bind Biotinylated Human IGF-I, His,Avitag (Cat. No. IG1-H82Q6) with an affinity constant of 68 nM as determined in a SPR assay (Biacore 8K) .

References
  • [1] Wang P, Mak V C Y, Cheung L W T. Drugging IGF-1R in cancer: new insights and emerging opportunities[J]. Genes & Diseases, 2022.https://doi.org/10.1016/j.gendis.2022.03.002.
  • [2] Lin S L, Lin C Y, Lee W, et al. Mini Review: Molecular Interpretation of the IGF/IGF-1R Axis in Cancer Treatment and Stem Cells-Based Therapy in Regenerative Medicine[J]. International Journal of Molecular Sciences, 2022, 23(19): 11781.https://doi.org/10.3390/ijms231911781.
  • [3] Morrione A, Belfiore A. Obesity, Diabetes, and Cancer: The Role of the Insulin/IGF Axis; Mechanisms and Clinical Implications[J]. Biomolecules, 2022, 12(5): 612.https://doi.org/10.3390/biom12050612.
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