Recombinant Mouse CD59a/MAC-IP Protein (Fc Tag)
SKU: PKSM040522-50
Recombinant Mouse CD59a/MAC-IP Protein (Fc Tag)
| SKU # | PKSM040522 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | AA987121, Cd59, RP24-297H17.1, protectin |
| Species | Mouse |
| Expression Host | HEK293 Cells |
| Sequence | Met 1-Lys 95 |
| Accession | O55186 |
| Calculated Molecular Weight | 35.4 kDa |
| Observed Molecular Weight | 42 kDa |
| Tag | C-hFc |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 92 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
Background
Protectin, a complement regulatory protein, also known as CD59, or MIRL (membrane inhibitor of reactive lysis) is a small protein that inhibits the complement membrane attack complex by binding C5b678 and preventing C9 from binding and polymerizing. The amino-terminal 25 amino acids represented a typical signal peptide sequence and the carboxy-terminal hydrophobic amino acids were characteristic for phosphatidylinositol-anchored proteins.It was found that the CD59/Protectin antigen is a small protein sometimes associated with larger components (45 and 80 kD) in urine. CD59/Protectin antigen was released from the surface of transfected COS cells by phosphatidylinositol-specific phospholipase C, demonstrating that it is attached to the cell membrane by means of a glycolipid anchor; it is therefore likely to be absent from the surface of affected erythrocytes in the disease paroxysmal nocturnal hemoglobinuria.