Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind 6Ckine/CCL21 in a functional ELISA. Nagakubo, D. et al. (2003) J. Immunol. 171:553. When Recombinant Mouse 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 1.5-12 ng/mL. |
Source | Spodoptera frugiperda, Sf 21 (stably transfected)-derived mouse IGFBP-rp1/IGFBP-7 protein Ser28-Leu281, with an N-terminal 10-His tag |
Accession # | |
N-terminal Sequence | His |
Protein/Peptide Type | Recombinant Proteins |
Gene | Igfbp7 |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 27.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 35 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS and NaCl. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Insulin-like growth factor (IGF) binding protein-related protein 1 (IGFBP-rp1), also known as IGF binding protein-7 (IGFBP-7) and Mac25 is a 31 - 37 kDa secreted glycoprotein that belongs to the IGFBP superfamily of molecules (1, 2). Members of this superfamily are characterized by the presence of 10 ‑ 12 conserved cysteines in the first third of the molecule, and the partial conservation of an xCGCCxxC octapeptide motif that exists in an N‑terminal IGFBP domain (1, 3). Mouse IGFBP-7 cDNA encodes a 281 amino acid (aa) precursor protein that contains a putative 25 aa signal peptide and a 256 aa mature region. The mature protein contains an N‑terminal 43 aa IGFBP domain that is followed by a 52 aa Kazal-type serine proteinase inhibitor domain and a 105 aa C-terminal Ig-like C2‑type domain (4, 5). The molecule is known to contain about 4 kDa of carbohydrate and believed to undergo phosphorylation (6). Mature mouse IGFBP-7 is 95% and 91% aa identical to mature rat and human IGFBP-7, respectively. Cells known to express IGFBP-7 include osteoblasts, select skeletal muscle fibers, visceral and vascular smooth muscle cells, breast epithelium, ciliated epithelium, renal tubular epithelium, astrocytes and oligodendroglia, and vascular endothelium in all tissues except brain (7). IGFBP-7 will bind both IGF-I and insulin, albeit at low affinity. When bound to IGF-I, it participates in growth promoting effects (8). Alternatively, IGFBP-7 by itself is an inhibitor of cell proliferation (6). Thus, its function is unclear. It is known to bind heparin, syndecan-1 and chemokines (8, 9). Based on human studies and aa conservation in relevant regions, mouse IGFBP-7 might be be expected to undergo proteolytic cleavage extracellularly (8). This will create an 8 kDa, 72 aa subunit (containing the IGFBP domain) that is disulfide-linked to a 25 kDa, 184 aa C-terminal subunit. Cleavage will reduce IGF‑I bonding activity and the promotion of IGF‑dependent cell proliferation.
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