Recombinant Rat Tumor Necrosis Factor-alpha (rRtTNF-α)
Catalogue Numbers: PR3014-5, PR3014-20
Sizes: 5µg, 20µg
Source: Escherichia coli
Molecular Weight: Approximately 17.3 kDa. a single, non-glycosylated polypeptide chain containing 157 amino acids.
Purity: >95% by SDS-PAGE and HPLC analyses.
Biological Activity: Fully biologically active when compared to standard. The Specific Activity is ≥5.0 × 107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized from a 0.2mm filtered concentrated solution in 20mM PB, pH7.2, 150mM NaCl.
AA Sequence: MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV
VPADGLYLIY SQVLFKGQGC PDYVLLTHt V SRFATSYQEK VSLLSAIKSP
CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV
YFGVIAL
Endotoxin: Less than 1EU/mg of rRtTNF-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 USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China
Description: Tumor necrosis factor alpha (TNF-α), 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-α occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Two types of receptors for TNF-α have been described and virtually all cell types studied show the presence of one or both of these receptor types.