Recombinant Canine IL-3 protein
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.2 ng/ml, corresponding to a specific activity of > 5.0 × 106 IU/mg.
Less than 1 EU/μg of rCaIL-3 as determined by LAL method.
RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP
Approximately 14.0 kDa, a single non-glycosylated polypeptide chain containing 120 amino acids.
Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Interleukin-3 (IL-3) is a type of biological signal (cytokine) which is encoded by the IL-3 gene located on chromosome 5 and produced primarily by activated T cells beside human thymic epithelial cells, activated Mouse mast cells, Mouse keratinocytes and neurons/astrocytes. The protein acts in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. The canine IL-3 reported to be a monomer, as it is known, contains 120 amino acids residues which is a single non-glycosylated polypeptide. The canine IL-3 shares