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Recombinant Human Hemopexin/HPX Protein (His Tag)(Active)
SKU: PKSH031380-100
Recombinant Human Hemopexin/HPX Protein (His Tag)(Active)
| SKU # | PKSH031380 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | Hemopexin, Hpx, Hpxn |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Met 1-His 462 |
| Accession | NP_000604.1 |
| Calculated Molecular Weight | 50.7 kDa |
| Observed Molecular Weight | 70-75 kDa |
| Tag | C-His |
| Bio-activity | Measured by its ability to bind protoporphyrin IX (PPPIX). Recombinant human Hemopexin binds > 10 μM PPPIX, resulting in a 50% decrease in the fluorescence signal of human Hemopexin. |
Properties
| Purity | > 96 % 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
Hemopexin (HPX) is plasma glycoprotein belongs to the family of the acute-phase proteins whose synthesis is induced after an inflammatory event. Hemopexin with two four-bladed beta -propeller folds has been found in other proteins including collagenases and provides sites for protein-protein interactions. The liver is the major synthesizing organ. Hemopexin participates in maintaining and recycling the iron pool by utilizing its high binding affinity toward heme composed of protoporphyrin IX and iron. It also functions in preventing oxidation caused by heme after hemolysis. Hydrophobic heme molecules can intercalate into lipid membranes and participate in the oxidation of lipid membrane components through the Fenton reaction resulting in lipid peroxidation. Hemopexin undergoes a conformational change upon the binding of heme. The conformational change allows hemopexin to interact with a specific receptor, forming a complex which is then internalized. Heme concentrations in plasma increase after hemolysis, which is associated with several pathological conditions such as reperfusion injury and ischemia.