C22-103-01 rHuTNF-1說明書

Catalog Number:  C22-103-01
Source:  Escherichia coli.
Molecular Weight:  Approximately 17.5 kDa, a single non-glycosylated polypeptide chain containing 158 amino acids.
Quantity:  10_g/50_g/1000_g
AA Sequence:  MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV
 VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS
 PCQRETPEGA EAKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ
 VYFGIIAL
Purity:  >95% by SDS-PAGE and HPLC analyses.
Biological Activity:  Fully biologically active when compared to standard. The ED50 determined by a cytotoxicity assay using murine L929 cells is less than 0.05 ng/ml, corresponding to a specific activity of＞2.0 ×107 IU/mg in the presence of the metabolic inhibitor actinomycin D.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized from a 0.2μm filtered concentrated solution in 20mM PB 10mM Nacl, pH 7.0.
Endotoxin: Less than 1EU/μg of rHuTNF-α as determined by LAL method.
Reconstitution:    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.
Storage:  This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage,
 preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For
 maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to
 -70°C. Avoid repeated freeze/thaw cycles.
Usage:  This material is offered by Shanghai Corning Bio-Tech for research, laboratory or further
 evaluation purposes. NOT FOR HUMAN USE.

Human Tumor Necrosis Factor-alpha
Tumor necrosis factor alpha (TNF-@), also called cachectin, is produced by neutrophils, activated lymphocytes, macrophages,
NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. TNF-@ occurs as a secreted,
soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF-@ is
glycosylated, but non-glycosylated recombinant TNF-@ has comparable biological activity. The biologically active native form of
TNF-@ is reportedly a trimer. Human and murine TNF-@ show approximately 79% homology at the amino acid level and
crossreactivity between the two species. Two types of receptors for TNF-@ have been described and virtually all cell types
studied show the presence of one or both of these receptor types.