Protein S100-A11(S100A11) is a member of the S-100 family. S100A11 is widely expressed in multi pletissues, and is located in cytoplasm, nucleus, and even cell periphery. S100A11 exists as a non-covalent homodimer with an antiparallel conformation. Ca(2+) binding to S100A11 would trigger conformational changes which would expose the hydrophobic cleft of S100A11 and facilitate its interaction with target proteins. As a dual cell growth mediator, S100A11 acts as either a tumor suppressor or promoter in many different types of tumors and would play respective roles in influencing the proliferatin of the cancer cells. In the nucleus, S100A11 suppresses the growth of keratinocytes through p21 (CIP1/WAF1) activation and induces cell differentiation. S100A11 is also a novel diagnostic marker in breast carcinoma.
Recombinant Mouse S100A11 Protein (His Tag)(Active)
From: £49.60
Size | 10µg, 50µg |
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Active Protein | Active protein |
Activity | Immobilized Human ANXA2(Cat: PKSH032074) at 10μg/ml(100 μl/well) can bind Mouse S100A11-His. The ED50 of Mouse S100A11-His is 0.8μg/mL. |
Protein Construction | Recombinant Mouse S100-A11 is produced by our E.coli expression system and the target gene encoding Met1-Ile98 is expressed with a 6His tag at the N-terminus. |
Sequence | Met1-Ile98 |
Fusion Tag | N-His |
Accession | P50543 |
Species | Mouse |
Expressed Host | E.coli |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Purity | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg 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. |
Mol Mass | 12.6 kDa |
AP Mol Mass | 12 kDa |
Formulation | Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4. |
Research Areas | |
Reconstitution | Please refer to the printed manual for detailed information. |