Recombinant Mouse S100A4 Protein (His Tag) | PKSM041285

Recombinant Mouse S100A4 Protein (His Tag) | PKSM041285 | Gentaur US, UK & Europe Disrtribition

Synonyms: Protein S100-A4; Metastasin; Metastatic cell protein; PEL98; Placental calcium-binding protein; Protein 18A2; Protein Mts1; S100 calcium-binding protein A4; S100a4; Capl; Mts1

Active Protein: N/A

Activity: Recombinant Mouse S100-A4 is produced by our E.coli expression system and the target gene encoding Met1-Lys101 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Mouse S100-A4 is produced by our E.coli expression system and the target gene encoding Met1-Lys101 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-His

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.

Molecular Mass: 12.5 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: S100A4 is a member of the S100 family of proteins. The S100 family is further classified as a member of the EF-hand superfamily of Ca++-binding proteins. These participate in both calcium-dependent and calcium-independent protein-protein interactions. The hallmark of this superfamily is the EF-hand motif that consists of a Ca++-binding site flanked by two α-helices (helix E and helix F) that were originally identified in a right-handed model of carp muscle calcium-binding protein. Mouse S100A4 is 101 amino acids (aa) in length. It contains two EF hand domains, one between aa 12-47, and a second between aa 50-85. S100A4 activity has been associated with cell transformation. It seems likely this is either coincidental, or a consequence, rather than a cause of transformation.

Research Area: N/A