Measured by its ability to neutralize IGF‑II-induced proliferation in the MCF‑7 human breast cancer cell line. Karey, K.P. et al. (1988) Cancer Research 48:4083. The Neutralization Dose (ND50) is typically 2-12 µg/mL in the presence of 14 ng/mL Recombinant Human IGF‑II.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Cell Proliferation Induced by IGF‑II and Neutralization by Human IGF-II Antibody.
Recombinant Human IGF‑II (Catalog # 292-G2) stimulates proliferation in the MCF‑7 human breast cancer cell line in a dose-dependent manner (orange line), as measured by Resazurin (Catalog # AR002). Proliferation elicited by Recombinant Human IGF‑II (14 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human IGF-II Monoclonal Antibody (Catalog # MAB292). The ND50 is typically 2-12 µg/mL.
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 and somatomedin A) and insulin-like growth factor II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved (100% identity between human, bovine, and porcine proteins) and exhibit cross-species activity.
IGF-II is a potent mitogenic growth factor. However, unlike IGF-I which has important postnatal roles, the growth-promoting function of IGF-II is limited to embryonic development.
Two specific cell surface receptors that bind IGF-I and IGF-II have been identified. The type I IGF receptor that participates in IGF signaling is structurally related to the insulin receptor. It is a disulfide-linked heterotetrameric transmembrane glycoprotein with an intracellular tyrosine kinase domain. Type I IGF receptor binds IGF-I with higher affinity than IGF-II. The type II IGF receptor which binds IGF-II with much higher affinity than IGF-I is also the cation-independent mannose 6-phosphate receptor. At the present time, it is not known if the type II IGF receptor participates in the IGF signaling pathway. An additional unknown receptor which mediates IGF‑II signaling has also been proposed. Circulating IGFs exist in complexes bound to IGF binding proteins. Currently, at least six high affinity binding proteins have been identified.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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