Recombinant Mouse TNF-alpha, Animal-Free Protein
Recombinant Mouse TNF-alpha, Animal-Free Protein Summary
Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Product Specifications
Leu80-Leu235, with an N-terminal Met & Ser84-Leu235
Produced using non-animal reagents in an animal-free laboratory.
Analysis
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Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AFL410
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 0.2 mg/mL in sterile PBS. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
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Background: TNF-alpha
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, immune system development, apoptosis, and lipid metabolism (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. TNF-alpha is produced by a wide variety of immune, epithelial, endothelial, and tumor cells (1, 2). TNF-alpha is assembled intracellularly to form a noncovalently linked homotrimer which is expressed on the cell surface (4). Cell surface TNF-alpha can induce the lysis of neighboring tumor cells and virus infected cells, and it can generate its own downstream cell signaling following ligation by soluble TNFR I (2, 5). Shedding of membrane bound TNF-alpha by TACE/ADAM17 releases the bioactive cytokine, a 55 kDa soluble trimer of the TNF-alpha extracellular domain (6-8). TNF-alpha binds the ubiquitous 55-60 kDa TNF RI (9, 10) and the hematopoietic cell-restricted 80 kDa TNF RII (11, 12), both of which are also expressed as homotrimers (1, 2, 13). Both type I and type II receptors bind TNF-alpha with comparable affinity (14), although only TNF RI contains a cytoplasmic death domain which triggers the activation of apoptosis. Soluble forms of both types of receptors are released and can neutralize the biological activity of TNF-alpha (15).
- Zelova, H. and J. Hosek (2013) Inflamm. Res. 62:641.
- Juhasz, K. et al. (2013) Expert Rev. Clin. Immunol. 9:335.
- Fransen, L. et al. (1985) Nucleic Acids Res. 13:4417.
- Tang, P. et al. (1996) Biochemistry 35:8216.
- Perez, C. et al. (1990) Cell 63:251.
- Black, R.A. et al. (1997) Nature 385:729.
- Moss, M.L. et al. (1997) Nature 385:733.
- Gearing, A.J.H. et al. (1994) Nature 370:555.
- Schall, T.J. et al. (1990) Cell 61:361.
- Loetscher, H. et al. (1990) Cell 61:351.
- Dembic, Z. et al. (1990) Cytokine 2:231.
- Smith, C.A. et al. (1990) Science 248:1019.
- Loetscher, H. et al. (1991) J. Biol. Chem. 266:18324.
- Pinckard, J.K. et al. (1997) J. Biol. Chem. 272:10784.
- Engelmann, H. et al. (1990) J. Biol. Chem. 265:1531.
Manufacturing Specifications
Animal-Free Manufacturing ConditionsOur dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
FAQs
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