>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.01 EU per 1 μg of the protein by the LAL method.
Measured by its ability to bind 6Ckine/CCL21 in a functional ELISA. Nagakubo, D. et al. (2003) J. Immunol. 171:553. When Recombinant Human (rh) IGFBP-rp1/IGFBP-7 is immobilized at 500 ng/mL (100 μL/well), the concentration of Recombinant Human CCL21/6Ckine (Catalog # 366-6C) that produces 50% optimal binding response is found to be approximately 4-20 ng/mL.
Mouse myeloma cell line, NS0-derived human IGFBP-rp1/IGFBP-7 protein Asp30-Leu282, with an N-terminal 10-His tag
Recombinant Human IGFBP-rp1/IGFBP-7 (Catalog # 1334-B7) binds Recombinant CCL21/6Ckine in a functional ELISA. When Recombinant Human IGFBP-rp1/IGFBP-7 is immobilized at 500 ng/mL (100 µL/well), the concentration of Recombinant Human CCL21/6Ckine (Catalog # 366-6C) that produces 50% of the optimal binding response is approximately 4-20 ng/mL.
1 μg/lane of Recombinant Human IGFBP-rp1/IGFBP-7 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 36 kDa.
IGFBP-rp1, also known as Mac25/Angiomodulin (AGM), tumor-derived adhesion factor (TAF) and prostacyclin-stimulating factor (PSF), is a secreted protein that contains three protein domain modules. Human IGFBP-rp1 cDNA encodes 282 amino acid (aa) residue precursor protein with a putative 26 aa signal peptide. Mature IGFBP-rp1 is a glycosylated protein with an N-terminal IGFBP domain, followed by a Kazal-type serine proteinase inhibitor domain and a C-terminal immunoglobulin-like C2-type domain. The similarity of IGFBP-rp1 with the IGFBPs is confined to the N-terminal IGFBP domain, which contains all 12 of the conserved cysteine residues found in IGFBP1 through 5. Human and mouse IGFBP-rP1 are highly homologous. Human and mouse IGFBP-rp1 share 94% aa sequence identity. IGFBP‑rp1 is expressed in many normal tissues and in cancer cells. It is abundantly expressed in high endothelial venules (HEVs) of blood vessels in the secondary lymphoid tissues. The expression of IGFBP-rp1 is upregulated in senescing epithelial cells and by retinoic acid. IGFBP-rp1 binds IGF and insulin with very low affinity and has been shown to enhance the mitogenic actions of IGF and insulin. IGFBP-rp1 also has IGF/insulin-independent activities. It interacts with heparan sulfate proteoglycans, type IV collagen, and specific chemokines. IGFBP-rp1 supports weak cell adhesion, promotes cell spreading on type IV collagen, and stimulates the production of the potent vasodilator PGI2.. It modulates tumor cell growth and has also been implicated in angiogenesis. IGFBP-rp1 is proteolytically cleaved between lysine 97 and alanine 98. Cleaved IGFBP-rp1 has enhanced cell attachment activity but can no longer bind IGF/insulin (1 - 3).
Hwa, V. et al. (1999) Endocrinology Rev. 20:761.
Nagakubo, D. et al. (2003) J. Immunol. 171:553.
Ahmed, S. et al. (2003) Biochem. Biophys. Res. Commun. 310:612.
Insulin-like Growth Factor Binding Protein Related Protein 1
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