Anti-Human IGF-II

Purified Recombinant Human IGF-11 (>98%)

This antigen affinity purified polyclonal antibody has been 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 containing 5.0% w/v trehalose with no calcium, magnesium, or preservatives present.

The lyophilized antigen affinity purified polyclonal antibody can be stored desiccated at -20°C to -70°C for twelve months from date of receipt. The reconstituted antibody can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted antibody, aseptically aliquot into working volumes and store at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. No detectable loss of activity was observed after six months.

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Immunohistochemistry: Suitable for use at concentration of 5-15 µg/mL.
Neutralization: Measured by its ability to neutralize IGF-II/IGF2-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 0.2-0.8 µg/mL in the presence of 14 ng/mL Recombinant Human IGF-II/IGF2.

Rabbit Anti-Human Insulin Like Growth Factor-II (IGF-11) recognizes Human IGF-11. This antigen affinity purified polyclonal antibody was purified using a proprietary chromatographic technique that includes covalently immobilizing the antigen proteins or peptides to agarose based beads. This purification method enhances specificity, reduces nonspecific binding of extraneous IgG and provides you with the most reliable reagent available for your early discovery research.

Insulin-like growth factor 2 (IGF-2) is a polypeptide hormone with structural and functional homology with IGF-I and pro-insulin.¹ IGF-2 exerts its effects by binding to the IGF-1 receptor. IGF2 may also bind to the IGF-2 receptor. The major role of IGF2 is growth promoting hormone during gestation. IGF-2 has been shown to be an important regulator of fetoplacental growth.²

1. Hoeflich, A. et al. (1994) Hormone Research 41: 66
2. Gruslin, A. et al. (2005) Proc Natl Acad Sci U S A. 102(31):11047-52.