Detects mouse TNF-alpha in direct ELISAs and Western blots. In direct ELISAs, approximately 15% cross-reactivity with human TNF‑ alpha is observed, and less than 5% cross-reactivity with recombinant bovine TNF‑ alpha, recombinant canine TNF‑ alpha, recombinant equine TNF‑ alpha, recombinant feline TNF‑ alpha, and recombinant porcine TNF‑ alpha is observed.
Polyclonal Goat IgG
Protein A or G purified
E. coli-derived recombinant mouse TNF-alpha Leu80-Leu235 Accession # P06804
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize TNF‑ alpha -induced cytotoxicity in the L‑929 mouse fibroblast cell line [Matthews, N. and M.L. Neale (1987) in Lymphokines and Interferons, A Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 221]. The Neutralization Dose (ND50) is typically 0.2-0.6 µg/mL in the presence of 0.25 ng/mL Recombinant Mouse TNF‑ alpha and 1 µg/mL actinomycin D.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Cytotoxicity Induced by TNF‑ alpha and Neutralization by Mouse TNF‑ alpha Antibody. Recombinant Mouse TNF‑ alpha (Catalog # 410-MT) induces cytotoxicity in the the L‑929 mouse fibroblast cell line in a dose-dependent manner (orange line), as measured by crystal violet staining. Cytotoxicity elicited by Recombinant Mouse TNF‑ alpha (0.25 ng/mL) is neutralized (green line) by increasing concentrations of Mouse TNF‑ alpha Polyclonal Antibody (Catalog # AB-410-NA). The ND50 is typically 0.2-0.6 µg/mL in the presence of the metabolic inhibitor actinomycin D (1 µg/mL).
Preparation and Storage
Reconstitute at 1 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Tumor necrosis factor alpha (TNF-alpha, also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, apoptosis, and immune system development. TNF-alpha is produced by a wide variety of immune and epithelial cell types (1, 2). Mouse TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD) (3). Within the ECD, mouse TNF-alpha shares 94% aa sequence identity with rat and 70% - 77% with bovine, canine, cotton rat, equine, feline, human, porcine, rat, and rhesus TNF-alpha. The 26 kDa type 2 transmembrane protein is assembled intracellularly to form a noncovalently linked homotrimer (4). Ligation of this complex induces reverse signaling that promotes lymphocyte costimulation but diminishes monocyte responsiveness (5). Cleavage of membrane bound TNF-alpha by TACE/ADAM17 releases a 55 kDa soluble trimeric form of TNF-alpha (6, 7). TNF-alpha trimers bind the ubiquitous TNF RI and the hematopoietic cell-restricted TNF RII, both of which are also expressed as homotrimers (1, 8). TNF-alpha regulates lymphoid tissue development through control of apoptosis (2). It also promotes inflammatory responses by inducing the activation of vascular endothelial cells and macrophages (2). TNF-alpha is a key cytokine in the development of several inflammatory disorders (9). It contributes to the development of type 2 diabetes through its effects on insulin resistance and fatty acid metabolism (10, 11).
Idriss, H.T. and J.H. Naismith (2000) Microsc. Res. Tech. 50:184.
Hehlgans, T. and K. Pfeffer (2005) Immunology 115:1.
Fransen, L. et al. (1985) Nucl. Acids Res. 13:4417.
Tang, P. et al. (1996) Biochemistry 35:8216.
Eissner G. et al. (2004) Cytokine Growth Factor Rev. 15:353.
Black, R.A. et al. (1997) Nature 385:729.
Moss, M.L. et al. (1997) Nature 385:733.
Loetscher, H. et al. (1991) J. Biol. Chem. 266:18324.
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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