Human IGF-2 ELISA

Features

• European Union: for in vitro diagnostic use
• Rest of the world: for research use only!
• duration: 3h
• calibrated against the International Standard: WHO NIBSC 96/538
• Inter- and Intra-Assay CV < 10%
• 5 single Calibrators: 0.45 - 9 ng/mL, lyophilized, human recombinant IGF-II
• 2 Controls, lyophilised
• limit of detection 0.06 ng/mL

Research topic

Growth hormone and factor-related products

Summary

The insulin-like growth factors (IGF)-I and –II play a pivotal role in the regulation of proliferation and differentiation of several tissue types (1-3). IGF-I also called Somatomedin C (4) has a molecular weight of 7.469 kDa (5). Its expression is mainly regulated by Growth Hormone and nutrition (6). But several hormones and peptide factors are known to influence IGF-II synthesis in different tissues. Bioavailability of the IGFs is regulated by specific binding proteins (IGFBP). Beside the high affinity Insulin-like Growth Factor Binding Proteins 1-6, IGFs are also bound be IGFBP-related Proteins (7, 8, 22). These binding proteins bind IGF-I and IGF-II with the same affinity or prefer IGF-II (9, 10). Direct measurement of IGFs in serum samples without pretreatment results in false values because of the extremely slow dissociation of the IGF/IGFBP complexes during the assay incubation only a part of the IGF-II in the specimen can bind to the antibodies and be detected. Therefore, various techniques were applied to physically separate IGF-II from its binding proteins before measurement, including (a) size exclusion chromatography under acidic conditions, (b) solid-phase extraction and (c) acid-ethanol extraction (2, 12, 13) These techniques, however, are either inconvenient or time-consuming or give incomplete and notreproducible recoveries. This assay is easy, fast and results do not depend on the binding protein concentration of the sample. It is based on the high specificity of the employed antibodies for IGF-II. There is virtually no cross-reactivity with IGF-I. This allows the separation of IGF-II from the binding proteins by acidification and blocking of the free binding proteins with IGF-I. Thus, the endogenous IGF-II is free in solution (15, 21, 23). Indication Scientific studies in the context of neonatal hypertrophy or hypotrophy (IGF-II is a fetal growth factor) and malignancy (IGF-II is an oncogenic growth factor). Age-related reference values are shown in Table 1. IGF-II appears to be suitable for differential diagnosis in various malignant diseases. For example, IGF-II can be used to differentiate between adrenocortical tumors and adenomas. In prostate cancer, too, tumor staging and the differentiation between carcinoma and hyperplasia can be improved by measuring IGF-II in serum (24, 25). Recent results from neurology show that the IGF system is also important in the development of Alzheimer's and Parkinson's disease (26).