The purity of recombinant mTNF-α was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant mTNF-α and staining overnight with Coomassie Blue.Learn more about how we get our images
The viability of L-929 cells treated with increasing concentrations of mTNF-α in the presence of 2 ng/ml actinomycin D was assessed. Cells were stained with crystal violet at the end of treatment and the OD595 was determined.Learn more about how we get our images
Western blot analysis of extracts from HeLa cells, untreated or treated with mouse TNF-α for 20 minutes, using Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb #4370 (upper) and p44/42 MAPK (Erk1/2) (137F5) Rabbit mAb #4695 (lower).Learn more about how we get our images
Recombinant mouse TNF-α (mTNF-α) Leu80-Leu235 (Accession #NP_038721) was expressed in human 293 cells at Cell Signaling Technology.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mTNF-α. All lots are greater than 98% pure.
Based on amino acid sequencing, greater than 50% of recombinant mTNF-α starts at Leu80 (LRSSS) and has a calculated MW of 17,257. The remainder starts at Ser82 (SSSQN). DTT-reduced and non-reduced protein migrate as 16 kDa polypeptides.
The bioactivity of recombinant mTNF-α was determined in a L-929 cell viability assay. The ED50 of each lot is between 2-8 pg/ml.
Less than 0.01 ng endotoxin/1 μg mTNF-α.
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 20 μg BSA per 1 μg mTNF-α. Carrier free: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2.
Stable in lyophilized state at 4°C for 1 year after receipt. Sterile stock solutions reconstituted with carrier protein are stable at 4°C for 2 months and at -20°C for 6 months. Avoid repeated freeze-thaw cycles.Maintain sterility. Storage at -20°C should be in a manual defrost freezer.
TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, ERK (p44/42), p38 MAPK and NF-κB) promotes the survival of cells, while TNF-α mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3).
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