| 货号 | AF1824-SP |
| 别名 | Adipsin; ADN; ADNcomplement factor D; AMBP-1; C3 convertase activator; CFD; complement factor D (adipsin); complement factor D preproprotein; D component of complement (adipsin); DF; EC 3.4.21; EC 3.4.21.46; PFD; Properdin factor DADIPSIN |
| 反应种属 | Human |
| 应用 | Western Blot(0.1 µg/mL) Immunoprecipitation(25 µg/mL) |
| 目标/特异性 | Detects human Complement Factor D in direct ELISAs and Western blots. In direct ELISAs, approximately 10% cross-reactivity with recombinant mouse Complement Factor D is observed, and less than 1% cross-reactivity with recombinant human (rh) Complement Factor B and rhComplement Factor I is observed. |
| 使用方法 | Western Blot: 0.1 µg/mL Immunoprecipitation: 25 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 | 1675 (Human); 11537 (Mouse); 54249 (Rat) |
| 应用文献 | |
| R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function. | |
| 纯化方式 | Antigen Affinity-purified |
| 免疫原 | Mouse myeloma cell line NS0-derived recombinant human Complement Factor D Ile26-Ala253 Accession # P00746 |
| 生物活性 | Human |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 背景 | Complement Factor D is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. Expressed in adipose tissue at high levels, factor D is also known as adipsin (1). It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3 (2). Factor D protease activity is regulated by reversible conformational changes, which differs from the majority of serine proteases whose regulation involves either activation by processing of the zymogens or inactivation by binding of the inhibitors. Compared to its physiologically important proteolytic activity, factor D has much lower activity toward synthetic peptide substrates. However, thioester substrates have been routinely used for assessing factor D activity (3). |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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