HUMAN IGFBP-3 Chemical Properties

storage temp. 

−20°C

form 

lyophilized powder

color 

white to off-white

biological source

human

Safety Information

Hazard Codes 

T,C,F

Risk Statements 

23/24/25-36/37/38-52/53-35-20/21/22-11

Safety Statements 

26-36/37/39-45-61

WGK Germany 

3

MSDS

• Language:English Provider:SigmaAldrich

HUMAN IGFBP-3 Usage And Synthesis

Uses

IGF-Binding Protein-3 human has been used to study its association with follicular fluid and subsequent effect on embryo development.

Biological Activity

IGFBP3 (insulin-like growth factor-binding protein 3) is involved in cell survival as well as cell death and tumorigenesis. Epigenetic changes in IGFBP3 affect non-small-cell lung cancer, hepatocellular carcinoma, ovarian cancer, skin cancer, urological cancers, breast cancer and gastric cancer. IGFBP3 is a primary growth inhibitor and can reverse the mitogenic functions of IGF-1 (insulin like growth factor 1) by inducing apoptosis.IGFBP-3 functions both in an IGF-dependent and independent manner. Its IGF-dependent roles involve endocrine function by delivering IGFs to target cells and activating downstream signaling. Meanwhile, its IGF-independent roles include interactions with extracellular matrix and plasma membrane proteins, as well as translocation into the cytoplasm and nucleus. The C-terminal domain has cell-penetrating abilities, enabling the generation of short peptides for intracellular delivery of drugs or genes.

Description

IGFBP3 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids and having a molecular mass of 28806 Dalton.
IGFBP-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli

Background

IGFBP3 is a member of the IGFBP family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with IGFALS and either IGF I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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