Recombinant Human ENTPD3/NTPDase3/CD39L3 Protein (His Tag) (PKSH031361)
For research use only.
| Synonyms | CD39L3, HB6, NTPDase-3 |
| Species | Human |
| Expression Host | Baculovirus-Insect Cells |
| Sequence | Gln 44-Pro 485 |
| Accession | O75355 |
| Calculated Molecular Weight | 51 kDa |
| Observed Molecular Weight | 50 kDa |
| Tag | C-His |
| Bio-activity | Measured by its ability to hydrolyze the 5'-phosphate group from the substrate adenosine-5'-triphosphate (ATP). The orthophosphate product is measured by a Malachite Green Phosphate Detection Kit. The specific activity is > 70, 000 pmol/min/µg. |
| Form | Liquid |
| Purity | > 97% as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Store at < -20℃, stable for 6 months. Please minimize freeze-thaw cycles. |
| Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
| Formulation |
Supplied as sterile 20 mM Tris, 500 mM NaCl, pH 7.4, 10% glycerol 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. |
| Background | The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. |
Note: Data for this module come from published literature that cites this product, displaying other products used together in the same research paper.
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