货号 | BAF1334 |
别名 | angiomodulin; FSTL2; IBP-7; IGFBP7; IGFBP-7; IGFBP-7PGI2-stimulating factor; IGFBP-7v; IGFBPRP1; IGFBP-rP1; insulin-like growth factor binding protein 7; insulin-like growth factor-binding protein 7; MAC25 protein; Mac25; MAC25IGF-binding protein 7; Prostacyclin-stimulating factor; PSF; PSFAGM; TAF; Tumor-derived adhesion factor | 全称 | Insulin-like Growth Factor Binding Protein Related Protein 1 |
反应种属 | Human |
应用 | Western Blot(0.1 µg/mL) Immunohistochemistry(5-15 µg/mL) |
目标/特异性 | Detects human IGFBP-rp1/IGFBP-7 in Western blots. In Western blots, less than 1% cross-reactivity with recominant human (rh) IGFBP-1, rhIGFBP-2, rhIGFBP-3, rhIGFBP-4, rhIGFBP-5 and rhIGFBP-6 is observed. |
使用方法 | Western Blot: 0.1 µg/mL Immunohistochemistry: 5-15 µg/mL |
来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 3490 (Human); 29817 (Mouse) |
纯化方式 | Antigen Affinity-purified |
免疫原 | Mouse myeloma cell line NS0-derived recombinant human IGFBP-rp1/IGFBP-7 Arg98-Arg277 Accession # AAA16187 |
生物活性 | Human |
标记 | Biotin |
溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
背景 | 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. Discounting a segment of 43 aa near the N-terminus that is missing in the mouse homologue, 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). |
运输条件 | Blue Ice |
存放说明 | -20℃ |
参考文献 |
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