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| カタログ番号 | HC440026 |
|---|---|
| 説明 |
Simlukafusp alfa (HC440026) is a research-grade recombinant antibody targeting Surface-expressed protease. Produced in mammalian cells with native-like glycosylation.
Highlights
|
| 種反応性 | Human |
| アプリケーション | ELISA, Bioactivity: FACS, Functional assay, Research in vivo |
| 宿主種 | Human |
| クローン性 | Monoclonal |
| アイソタイプ | IgG1-kappa |
| 発現システム | Mammalian cells |
| テスト済みアプリケーション | WB, FCM |
| ターゲット | Surface-expressed protease, Gelatine degradation protease FAP, Integral membrane serine protease, Dipeptidyl peptidase FAP, Seprase, FAP, Post-proline cleaving enzyme, APCE, SIMP, FAPalpha, 170 kDa melanoma membrane-bound gelatinase, Fibroblast activation protein alpha, Serine integral membrane protease, Prolyl endopeptidase FAP |
| エンドトキシンレベル | < 10 EU/mg |
| 純度 | >95% purity as determined by SDS-PAGE. |
| 精製 | Protein A/G purified from cell culture supernatant. |
| アクセッション番号 | Q12884 |
| 形態 | Liquid |
| 保存バッファー | 0.01M PBS pH 7.4 データシートのハードコピーまたはロット固有のCOAに記載された具体的なバッファー情報を参照してください。 |
| 安定性と保存 | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| 背景 | Prolyl endopeptidase FAP (FAPalpha & IL2V) is a ~87 kDa protein. Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). 1. Lee, KN. et al. (2004) Blood 103, 3783-8. PMID: 14751930 2. Lee, KN. et al. (2006) Blood 107, 1397-404. PMID: 16223769 3. Edosada, CY. et al. (2006) The Journal of biological chemistry 281, 7437-44. PMID: 16410248 4. Edosada, CY. et al. (2006) FEBS letters 580, 1581-6. PMID: 16480718 5. Meadows, SA. et al. (2007) Biochemistry 46, 4598-605. PMID: 17381073 6. Aggarwal, S. et al. (2008) Biochemistry 47, 1076-86. PMID: 18095711 7. Huang, CH. et al. (2011) Journal of biochemistry 149, 685-92. PMID: 21288888 8. Keane, FM. et al. (2013) FEBS open bio 4, 43-54. PMID: 24371721 9. Levy, MT. et al. (1999) Hepatology (Baltimore, Md.) 29, 1768-78. PMID: 10347120 10. Mueller, SC. et al. (1999) The Journal of biological chemistry 274, 24947-52. PMID: 10455171 |
| 注意事項 | For research use only. Not suitable for clinical or therapeutic use. |
SEC-HPLC detection for Research Grade Simlukafusp alfa.
Detects FAP/FAPalpha in indirect ELISAs.
SDS-PAGE for Research Grade Simlukafusp alfa.
Flow-cytometry using FITC anti-human FAP&IL2V antibody. U87 cells were fixed and permeabilized, then stained with an irrelevant antibody (Blue Histogram) or an FITC anti-human FAP&IL2V monoclonal antibody (Catalog: HC440026, Yellow Histogram) at a concentration of 5 µg/ml for 30 mins at RT. After washing, cells analysed on a NovoCyte Flow Cytometer.
Flow-cytometry using anti-human FAP antibody. Untransfected cells (blue Histogram) and Transfected cells (Yellow Histogram) were stained with an anti-human FAP monoclonal antibody (Catalog: HC440026) at a concentration of 5 µg/ml for 30 mins at RT. After washing, bound antibody was detected using a Goat Anti-Human IgG H&L Polyclonal Antibody, FITC (abinScience: HF690414) and cells analysed on a NovoCyte Flow Cytometer.
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