Recombinant Human IGFBP-rp1/IGFBP-7 Protein, CF

Recombinant Human IGFBP-rp1/IGFBP-7 Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: IGFBP-rp1/IGFBP-7

IGFBP-rp1, also known as IGFBP-7, 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 up-regulated 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).

Related Research Areas

• IGF Family
• Metabolic Peptide Hormones and Regulators