| Product Name | Human PRAME family member 1 (PRAMEF1) ELISA Kit |
|---|---|
| Description | PRAMEF1, Belongs to the PRAME family.Contains 2 LRR (leucine-rich) repeats.A leucine-rich repeat (LRR) is a protein structural motif that forms an _/_ horseshoe fold. It is composed of repeating 20_30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues. Leucine-rich repeats are frequently involved in the formation of protein_protein interactions. This assay has high sensitivity and excellent specificity for detection of Human PRAMEF1. No significant cross-reactivity or interference between Human PRAMEF1 and analogues was observed. |
| Synonyms | RP5-1198H6.2, RP5-845O24.1, dJ1198H6.1, |
| Method | Sandwich ELISA |
| Detection Range | 0.156-10 ng/mL |
| Sensitivity | 0.061 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | PRAMEF1, Belongs to the PRAME family.Contains 2 LRR (leucine-rich) repeats.A leucine-rich repeat (LRR) is a protein structural motif that forms an _/_ horseshoe fold. It is composed of repeating 20_30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues. Leucine-rich repeats are frequently involved in the formation of protein_protein interactions. |
| Supplier | Abebio |
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