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Recombinant Human BVES/POPDC1 Protein (GST Tag)
SKU: PKSH030823-100
Recombinant Human BVES/POPDC1 Protein (GST Tag)
| SKU # | PKSH030823 |
| Expression Host | E.coli |
Description
| Synonyms | HBVES, POP1, POPDC1 |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Met 1-Asn36 |
| Accession | NP_671488.1 |
| Calculated Molecular Weight | 30.8 kDa |
| Observed Molecular Weight | 32.2 kDa |
| Tag | N-GST |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 90 % as determined by reducing SDS-PAGE. |
| Endotoxin | Please contact us for more information. |
| 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
Ferritin, light polypeptide (FTL) is the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Storage of iron in the tissues occurs in the form of ferritin and hemosiderin. The latter originates from ferritin that has undergone intracellular digestion of its protein shell, leaving the iron core. Ferritin and hemosiderin are components of a continuum. Ferritin has been identified in all types of living organisms: animals, plants, molds, and bacteria. Whithin the protein shell of ferritin, iron is first oxidized to the ferric state for storage as ferric oxyhdroxide. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms.