Insulin-like growth factor (IGF) signaling plays a major role in regulating the proliferation and metabolism of normal and malignant cells. Insulin-like growth factor-binding proteins (IGFBPs) play an integral role in modifying IGF actions in a wide variety of cell types. The six IGFBP family members share a high affinity for IGF binding and are structurally related, but are encoded by distinct genes. IGF binding proteins can exert stimulatory or inhibitory effects by controlling IGF availability through high affinity binding of IGF at the carboxy-terminal domain. IGFBP3 is the most abundant serum IGF binding protein and the main mediator for IGF-I bioactivities. IGFBP3 also binds IGF-II, insulin, and other cellular and extracellular components to regulate cell growth, development, and apoptosis through both IGF-dependent and IGF-independent mechanisms. Research studies describe correlations between increased IGF-I levels and reduced levels of IGFBP3 with increased risks of developing cancer, including breast, colon, lung, and prostate cancer.

Insulin-like growth factor-binding protein 3; IBP-3; IGF-binding protein 3; IGFBP-3; IGFBP3; IBP3

p17936

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 40 kDa

Rabbit

IGFBP-3(Phospho-Ser183) polyclonal antibody detects endogenous levels of IGFBP-3 protein only when phosphorylated at Ser183.

Synthetic phosphopeptide derived from human IGFBP-3 around the phosphorylation site of Serine 183

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.