Recombinant Mouse CD59a/MAC-IP Protein (Fc Tag) | PKSM040522

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SKU:
575-PKSM040522
€998.00
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Description

Recombinant Mouse CD59a/MAC-IP Protein (Fc Tag) | PKSM040522 | Gentaur US, UK & Europe Disrtribition

Synonyms: AA987121;Cd59;protectin;RP24-297H17.1

Active Protein: N/A

Activity: A DNA sequence encoding the mouse CD59a (O55186) (Met 1-Lys 95), without the pro peptide, was fused with the Fc region of human IgG1 at the C-terminus.

Protein Construction: A DNA sequence encoding the mouse CD59a (O55186) (Met 1-Lys 95), without the pro peptide, was fused with the Fc region of human IgG1 at the C-terminus.

Fusion Tag: C-Fc

Species: Mouse

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 92 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and 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.

Molecular Mass: 35.4 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

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.

Research Area: N/A

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