Recombinant Human S100A1 Protein(Gst Tag) (PDEH100558)
For research use only.
| Synonyms | Bpb, NEF, Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 alpha, S100 beta, S100 calcium binding protein A1, S100 calcium binding protein B, S100 calcium-binding protein A1, S100 protein alpha polypeptide, S100A, s100a1, S100B, S100beta, S10A1 |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Met1-Ser94 |
| Accession | P23297 |
| Calculated Molecular Weight | 28.18 kDa |
| Observed Molecular Weight | 40 kDa |
| Tag | N-GST |
| Bio-activity | Not validated for activity |
| Purity | > 90% as determined by reducing SDS-PAGE. |
| Endotoxin | < 10 EU/mg 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 a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol. |
| Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis. |
| Background | Small calcium binding protein that plays important roles in several biological processes such as Ca2+ homeostasis, chondrocyte biology and cardiomyocyte regulation (PubMed:12804600). In response to an increase in intracellular Ca2+ levels, binds calcium which triggers conformational changes (PubMed:23351007). These changes allow interactions with specific target proteins and modulate their activity (PubMed:22399290). Regulates a network in cardiomyocytes controlling sarcoplasmic reticulum Ca2+ cycling and mitochondrial function through interaction with the ryanodine receptors RYR1 and RYR2, sarcoplasmic reticulum Ca2+-ATPase/ATP2A2 and mitochondrial F1-ATPase (PubMed:12804600). Facilitates diastolic Ca2+ dissociation and myofilament mechanics in order to improve relaxation during diastole. |
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