AF/LE Purified Anti-Human CD206 Antibody[15-2] (E-AB-F11610)
![AF/LE Purified Anti-Human CD206 Antibody[15-2] - 1](http://file.elabscience.com/assets/images/loading.png)
For research use only.
Conjugation: None (AF/LE)
APC Elab Fluor®700 FITC None (AF/LE) Unconjugated Show More
| Verified Samples | Verified Samples in FCM: HEK293T cells transfected with pcDNA3.1 plasmid encoding Human CD206 gene |
| Dilution | FCM 2 μg/mL(0.5×106-1×106 cells) |
| Isotype | Mouse IgG1, κ |
| Host | Mouse |
| Reactivity | Human |
| Applications | FCM |
| Clonality | Monoclonal |
| Immunogen | Recombinant Human CD206 protein |
| Abbre | CD206 |
| Synonyms | MRC, C type lectin domain family 13 member D, CD 206, CD206 antigen, C-type lectin domain family 13 member D, C-type lectin domain family 13 member D-like, Macrophage mannose receptor, Macrophage mannose receptor 1, Macrophage mannose receptor 1 like protein 1, Macrophage mannose receptor 1-like protein 1, Mannose receptor C type 1, Mannose receptor C type 1 like 1, MRC 1, OTTHUMP00000045206, MRC1L, bA541I, MRC1, CD206, CLEC13D, CLEC13DL, MMR, MRC1L1, bA541I19.1, hMR |
| Swissprot | |
| Cellular Localization | Endosome membrane, Cell membrane |
| Concentration | ≥ 1 mg/mL |
| Buffer | Sterile PBS, pH 7.2. < 1.0 EU per mg of the antibody as determined by the LAL method. |
| Purification Method | >98%, Protein A/G purified |
| Research Areas | Immunology, CDs |
| Clone No. | 15-2 |
| Conjugation | None (AF/LE) |
| Storage | Store at 4°C valid for 12 months or -20°C valid for long term storage, avoid freeze / thaw cycles. This preparation contains no preservatives, thus it should be handled under aseptic conditions. |
| Shipping | Ice bag |
| background | The recognition of complex carbohydrate structures on glycoproteins is an important part of several biological processes, including cell-cell recognition, serum glycoprotein turnover, and neutralization of pathogens. The protein encoded by this gene is a type I membrane receptor that mediates the endocytosis of glycoproteins by macrophages. The protein has been shown to bind high-mannose structures on the surface of potentially pathogenic viruses, bacteria, and fungi so that they can be neutralized by phagocytic engulfment. |
| Cat.No. | Product Name | Clone No. |
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