The purity of recombinant hTNF-α was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant hTNF-α and staining overnight with Coomassie Blue.Learn more about how we get our images
The viability of L-929 cells treated with increasing amounts of hTNF-α in the presence of 2 ng/ml actinomycin D was determined. 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 treated with hTNF-α for 20 minutes, using Phospho-NF-κB p65 (Ser536) (93H1) Rabbit mAb #3033 (upper) and total NF-κB p65 Antibody #3034 (lower).Learn more about how we get our images
Recombinant human TNF-α (hTNF-α) Val77-Leu233 (Accession #HUMTNFAB) was produced in E. coli at Cell Signaling Technology.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hTNF-α. All lots are greater than 98% pure.
Recombinant hTNF-α does not have a Met on the amino terminus and has a calculated MW of 17,352. DTT-reduced and non-reduced protein migrate as 18 kDa polypeptides. The expected amino-terminal VRSSS of recombinant hTNF-α was verified by amino acid sequencing. TNF-α is a non-disulfide-linked homotrimer in solution as determined by chemical cross-linking.
The bioactivity of hTNF-α was determined in an L-929 cell viability assay. The ED50 of each lot is between 10-500 pg/ml.
Less than 0.01 ng endotoxin/1 μg hTNF-α.
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 20 μg BSA per 1 μg hTNF-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). The role of TNF-α in autoimmunity is underscored by blocking TNF-α action to treat rheumatoid arthritis and Crohn’s disease (1,2,4).
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|8902SC||10 µg (With Carrier)||$ 191.0|
|8902SF||10 µg (Carrier Free)||$ 191.0|