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| Product Name | IGFBP-3 PROLICIA |
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| Description | IGFBP-3 PROLICIA: 1. Introduction Insulin-like growth factors (IGF) I and II are peptides that are growth factors for a broad range of cell types. In serum and other body fluids more than 99 % of the IGF?s are bound to Insulin-like growth factor binding proteins (IGFBP?s). Six high affinity binding proteins have been characterised until today. In human serum IGFBP-3 has the highest concentration and more than 95 % of the IGF?s are bound to the single binding site of IGFBP-3. It prolongs the shelf life of IGF?s and is the main circulating reservoir for IGF-I and -II. The availability of IGF-I and -II is regulated by a complex system. Beside the regulation of the biosynthesis of the peptides another mechanism is to enhance the bioavailability by decreasing the affinity of the IGFBP?s. One of the mechanisms is the release of bound IGF?s from IGFBP?s by proteases, generating fragments with reduced or no affinity for the IGF?s. For IGFBP-3 there are reports on a number of proteolytical fragments of 30 kDa, 22 - 25 kDa and 16 kDa, with reduced or no detectable affinity for the IGF?s. IGFBP-3 proteolytic activities have initially been found in pregnancy serum. Later fragments have been detected in other body fluids (1). Increased proteolysis has been observed in malignancies, as e.g. breast cancer (3) and leukemia (8), in malnourished elderly people (4), in insulin dependent diabetes mellitus (5) and after extensive exercise (6). IGFBP-3 protease activity has been measured by different techniques as immunoblot and ligand blot (2, 3, 4, 5, 6, 7), substrate zymography (7), FPLC (8) or in assays using 125I-IGFBP-3 (10). The ibt IGFBP-3 PROLICIA uses glycosylated IGFBP-3 as a substrate. Only functional IGFBP-3, i.e. IGFBP-3 and fragments that can bind IGF?s are detected, but not the fragments that have lost the affinity to IGF-II. It combines the advantages of western-ligand blotting with the speed and convenience of an ELISA. Please note: The proteolytic activity of IGFBP-3 proteases may be affected by the presence or absence of IGF?s. There are differences in proteolysis of glycosylated and non-glycosylated IGFBP-3 as it is used commonly in the assays with I125-IGFBP-3 (10). The Assay Buffer contains BSA and may affect proteolysis. 2. Applications In complex samples of human origin, non-proteolysed intrinsic IGFBP-3 may be present even in samples containing IGFBP-3 proteases and could affect the results. Also, at least theoretically, free IGF?s may be present in a very high concentration and also could compete with the binding of IGFBP-3 to the biotinylated ligands. Therfeore it is necessary to perform appropriate controls in complex samples The comparison of biotinylated and non-biotinylated IGFBP-3 as a substrate in the IGFBP-3 PROLICIA showed (for details see Application Note IGF018), that the non-biotinylated IGFBP-3 is digested more rapidly by Plasmin, than the biotinylated IGFBP-3. It is concluded that use of the non-biotinylated IGFBP-3 as a substrate may be close to the conditions in the human body. In addition it has a broad measuring range and it has a high sensitivity.Therefore the assay is recommended for quantitative measurement of IGFBP-3 protease activities. |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | BP3PROLICIA |
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| Order / More Info | IGFBP-3 PROLICIA from IMMUNOLOGICAL & BIOCHEMICAL TESTSYSTEMS GmbH |
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| Product Specific References | n/a |
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