Catalog Number: C22-123-01 Source: Escherichia coli. Molecular Weight: Approximately 17.3 kDa. The recombinant murine TNF-α is a soluble 157 amino acid protein which corresponds to C-terminal extracellular domain of the full length transmembrane protein. Quantity: 5μg/20μg/1000μg AA Sequence: MLRSSSQNSSDKPVAHVVANHQVEEQLEWLSQRANALLANGMDLKDNQLVVPADGLYLV Y SQVLFKGQGC PDYVLLTHTV SRFAISYQEKVNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL Purity: >97% by SDS-PAGE and HPLC analyses. Biological Activity: Fully biologically active when compared to standard. The ED50 determined by a cytotoxicity assay usingmurine L929 cells is less than 0.1 ng/ml, corresponding to a specific activity of> 1.0 × 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 solution in PBS, pH 7.2. Endotoxin: Less than 1EU/μg of rMuTNF-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.
Mouse Tumor Necrosis Factor-alpha Tumor necrosis factor alpha (TNF-α) is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. Mouse TNF-α occurs as a membrane-anchored form. 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. Human and murine TNF-α show approximately 79% homology at the amino acid level and crossreactivity between the two species.
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