Recombinant Mouse CX3CL1/Fractalkine Protein (His Tag) (PKSM040991)

For research use only.
Synonyms | ABCD-3, C-X3-C motif chemokine 1, C3Xkine, CX3C membrane-anchored chemokine, CXC3, CXC3C, Cx3c, Fkn, Fractalkine, NTN, NTT, Neurotactin, SCYD1, Scyd1, Small-inducible cytokine D1 |
Species | Mouse |
Expression Host | HEK293 Cells |
Sequence | Gln25-Arg337 |
Accession | O35188 |
Calculated Molecular Weight | 34.3 kDa |
Observed Molecular Weight | 50-65 kDa |
Tag | C-His |
Bio-activity | Not validated for activity |
Purity | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg 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 of 20mM PB,150mM NaCl,pH7.4. 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 | Fractalkine(CX3CL1) is a single-pass type I membrane protein and belongs to the intercrine delta family. It consists of an extracellular NH2-terminal domain, a mucin-like stalk, a transmembrane α helix, and a short cytoplasmic tail. CX3CL1 exists in two forms: as a membrane-anchored or as a shed 80-95K glycoprotein. Soluble CX3CL1 is generated by limited proteolysis on the cell surface, and a disintegrin and metallopeptidase 10 (ADAM10) and ADAM17/tumor necrosis factor-α-converting enzyme (ADAM17/TACE) participate in this shedding. It has been suggested that ADAM10 acts in the constitutive shedding, and ADAM17 acts in response to cell activation. The protein may play a role in regulating leukocyte adhesion and migration processes at the endothelium. |
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