| 货号 | MAB23071-SP |
| 别名 | COLEC1; COLEC1collectin-1; Collectin-1; HSMBPC; Mannan-binding protein; mannose-binding lectin (protein C) 2, soluble (opsonic defect); mannose-binding lectin (protein C) 2, soluble; Mannose-binding lectin; mannose-binding protein C; MBL2; MBL2D; MBLmannan-binding lectin; MBP; MBP1; MBP1mannose-binding lectin 2, soluble (opsonic defect); MBP-C; MGC116832; MGC116833 | 全称 | Mannose Binding Lectin |
| 反应种属 | Human |
| 应用 | Blockade of Receptor-ligand Interaction |
| 目标/特异性 | Detects human MBL in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant mouse MBL-2 is observed. |
| 使用方法 | Blockade of Receptor-ligand Interaction: In a functional ELISA, 0.5-1.5 µg/mL of this antibody will block 50% of the binding of 8 μg/mL of Recombinant Human MBL (Catalog # 2307-MB) to immobilized mannan coated at 1 µg/mL (100 µL/well). At 20 μg/mL, this antibody will block >90% of the binding. |
| 来源 | Monoclonal Mouse IgG2A Clone # 285623 |
| 产品组分 |
| 供应商 | R&D Systems |
| Entrez Gene IDs | 4153 (Human) |
| 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. A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms. | |
| 纯化方式 | Protein A or G purified from hybridoma culture supernatant |
| 免疫原 | Mouse myeloma cell line NS0-derived recombinant human MBL Glu21-Ile248 Accession # AAH96182 |
| 内毒素水平 | <0.10 EU per 1 μg of the antibody by the LAL method. |
| 生物活性 | Human |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.5 mg/mL in sterile PBS. |
| 背景 | Human mannose/mannan-binding lectin (MBL; gene name MBL2; also called MBP-C) is a 25 kDa member of the collectin family of pattern-recognition molecules (1‑3). It is a secreted glycoprotein that is synthesized as a 248 amino acid (aa) precursor that contains a 20 aa signal sequence, a 21 aa cysteine-rich region (with three cysteines) a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates (3, 4). The molecule is O-glycosylated and contains multiple hydroxylated prolines and lysines (3, 5). Functionally, the molecule operates as a multimer/oligomer. The basic structural unit is a homotrimer. The homotrimer is created by the formation of interchain disulfide bonds among the cysteine-rich regions, plus a helical interaction of the collagen-like domains of each participating polypeptide (5). Mutations in the collagen region are known to interfere with proper trimer and subsequent oligomer formation (6). Once formed, the trimer, as a unit, oligomerizes with other trimers to form high molecular weight complexes. Although the exact nature of these complexes are unclear, it would appear that a three trimer complex (230 kDa) and a four trimer complex (305 kDa) constitute much of the circulating MBL (7). It is within the context of these oligomers that MBL performs its functions. After secretion by hepatocytes, oligomerized MBL will both associate with serine proteases (MASP-1, 2 & 3) and bind to bacterial carbohydrates. If the MBL complex is small, opsonization of bacreria occurs. If the complex is large, the MASPs are engaged and a complement attack complex is generated, destroying bound bacteria (3, 7, 8). Human MBL shares 63%, 61% and 65% aa identity with mouse, porcine and bovine MBL, respectively. |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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