IGF‑I in Human Placenta.
IGF‑I was detected in immersion fixed paraffin-embedded sections of human placenta using Goat Anti-Human IGF‑I Recombinant Monoclonal Antibody (Catalog # MAB2911) at 3 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in decidual cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Insulin-like growth factor I, also known as somatomedin C, is the dominant effector of growth hormone and is structurally homologous to proinsulin. Human IGF-I is synthesized as two precursor isoforms with N- and alternate C-terminal propeptides (1). These isoforms are differentially expressed by various tissues (1). The 7.6 kDa mature IGF-I is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF‑I shares 94% and 96% aa sequence identity with mouse and rat IGF-I, respectively (2), and exhibits cross-species activity. It shares 64% aa sequence identity with mature human IGF‑II. Circulating IGF‑I is produced by hepatocytes, while local IGF-I is produced by many other tissues in which it has paracrine effects (1). IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally (3). IGF-I regulates glucose and fatty acid metabolism, steroid hormone activity, and cartilage and bone metabolism (4-7). It plays an important role in muscle regeneration and tumor progression (1, 8). IGF-I binds IGF‑I R, IGF-II R, and the insulin receptor, although its effects are mediated primarily by IGF-I R (9). IGF-I association with IGF binding proteins increases its plasma half‑life and modulates its interactions with receptors (10).
Philippou, A. et al. (2007) In Vivo 21:45.
Sandberg-Nordqvist, A.C. et al. (1992) Brain Res. Mol. Brain Res. 12:275.
Guvakova, M.A. (2007) Int. J. Biochem. Cell Biol. 39:890.
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