TNF active protein

Recombinant Mouse TNF

Cat. Num. AAA4159938

• Gene Names: Tnf; DIF; Tnfa; TNF-a; TNFSF2; Tnlg1f; Tnfsf1a; TNFalpha; TNF-alpha
• Purity: >95% as determined by SDS-PAGE
• Synonyms: TNF; Recombinant Mouse TNF; TNF-alpha; TNF-a; Tumor necrosis factor ligand superfamily member 2; Cachectin; Tnfa; Tnfsf2; Tnf; Recombinant Mouse Tumor Necrosis Factor Alpha (TNF); TNF active protein

• Host: E Coli
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from 0.2 um filtered PBS solution, pH 7.0.
• Sequence Length: 219

• Bioactivity: The ED(50) was determined cytolysis of murine L929 cells in the presence of Actinomycin D is <= 0.05 ng/mL, corresponding to a specific activity of >= 3.0 x 10^7 units/mg.
• Endotoxin Level: <1.0 EU/ug of recombinant protein as determined by the LAL method.
• Reconstitution: A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
• Preparation and Storage: The lyophilized protein is stable for at least one year from date of receipt at-70 degree C. Upon reconstitution, this cytokine can be stored in working aliquots at 2-8 degree C for one month, or at-20 degree C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.

Testing Data

Testing Data

Related Product Information for TNF active protein

TNF is secreted by macrophages, monocytes, neutrophils, T cells, natural killer cells following their stimulation by bacterial lipopolysaccharides. Cells expressing CD4 secrete TNF-alpha while CD8(+) cells secrete little or no TNF-alpha. Stimulated peripheral neutrophilic granulocytes but also unstimulated cells and also a number of transformed cell lines, astrocytes, microglial cells, smooth muscle cells, and fibroblasts also secrete TNF. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL-2, GM-CSF, SP, Bradykinin, immune complexes, inhibitors of cyclooxygenase and PAF (platelet activating factor). Human TNF-alpha is a non-glycosylated protein of 17 kDa and a length of 157 amino acids. Murine TNF-alpha is N-glycosylated. Homology with TNF-beta is approximately 30%. TNF-alpha forms dimers and trimers.

NCBI and Uniprot Product Information

• NCBI GI #: 518831589
• NCBI GeneID: 21926
• NCBI Accession #: NP_001265530.1
• NCBI GenBank Nucleotide #: NP_001265530.1
• UniProt Accession #: P06804
• Molecular Weight: 17.0 kDa
• NCBI Official Full Name: tumor necrosis factor isoform 2
• NCBI Official Synonym Full Names: tumor necrosis factor
• NCBI Official Symbol: Tnf
• NCBI Official Synonym Symbols: DIF; Tnfa; TNF-a; TNFSF2; Tnlg1f; Tnfsf1a; TNFalpha; TNF-alpha
• NCBI Protein Information: tumor necrosis factor
• UniProt Protein Name: Tumor necrosis factor
• Protein Family: Tumor necrosis factor
• UniProt Gene Name: Tnf
• UniProt Synonym Gene Names: Tnfa; Tnfsf2; TNF-a; NTF; ICD1; ICD2
• UniProt Entry Name: TNFA_MOUSE

NCBI Description

This gene encodes a multifunctional proinflammatory cytokine that belongs to the tumor necrosis factor (TNF) superfamily. Members of this family are classified based on primary sequence, function, and structure. This protein is synthesized as a type-II transmembrane protein and is reported to be cleaved into products that exert distinct biological functions. It plays an important role in the innate immune response as well as regulating homeostasis but is also implicated in diseases of chronic inflammation. In mouse deficiency of this gene is associated with defects in response to bacterial infection, with defects in forming organized follicular dendritic cell networks and germinal centers, and with a lack of primary B cell follicles. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013]

Uniprot Description

TNF-a: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Homotrimer. Interacts with SPPL2B. Belongs to the tumor necrosis factor family.

Protein type: Apoptosis; Cytokine; Membrane protein, integral; Motility/polarity/chemotaxis

Cellular Component: cell surface; external side of plasma membrane; extracellular space; integral to membrane; integral to plasma membrane; intracellular; lipid raft; phagocytic cup; plasma membrane; recycling endosome; secretory granule

Molecular Function: cytokine activity; identical protein binding; protease binding; protein binding; tumor necrosis factor receptor binding

Biological Process: activation of MAPK activity; activation of MAPKKK activity; activation of NF-kappaB transcription factor; apoptosis; calcium-mediated signaling; caspase activation; cell activation; cell proliferation; cellular extravasation; chronic inflammatory response to antigenic stimulus; cortical actin cytoskeleton organization and biogenesis; defense response; defense response to bacterium; defense response to Gram-positive bacterium; detection of mechanical stimulus involved in sensory perception of pain; DNA damage response, signal transduction resulting in induction of apoptosis; extracellular matrix organization and biogenesis; glucose metabolic process; humoral immune response; induction of apoptosis via death domain receptors; inflammatory response; JNK cascade; leukocyte migration; leukocyte tethering or rolling; lipopolysaccharide-mediated signaling pathway; MAPKKK cascade; multicellular organismal development; negative regulation of cell proliferation; negative regulation of cytokine secretion during immune response; negative regulation of endothelial cell proliferation; negative regulation of glucose import; negative regulation of interleukin-6 production; negative regulation of L-glutamate transport; negative regulation of lipid catabolic process; negative regulation of mitotic cell cycle; negative regulation of myelination; negative regulation of myoblast differentiation; negative regulation of osteoblast differentiation; negative regulation of protein complex disassembly; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of viral genome replication; organ morphogenesis; osteoclast differentiation; positive regulation of action potential; positive regulation of apoptosis; positive regulation of caspase activity; positive regulation of cell adhesion; positive regulation of cell proliferation; positive regulation of chemokine biosynthetic process; positive regulation of chemokine production; positive regulation of chronic inflammatory response to antigenic stimulus; positive regulation of cytokine production; positive regulation of cytokine secretion; positive regulation of fever; positive regulation of hair follicle development; positive regulation of heterotypic cell-cell adhesion; positive regulation of humoral immune response mediated by circulating immunoglobulin; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of inflammatory response; positive regulation of interferon-gamma production; positive regulation of interleukin-18 production; positive regulation of interleukin-6 production; positive regulation of interleukin-8 biosynthetic process; positive regulation of interleukin-8 production; positive regulation of JNK activity; positive regulation of JNK cascade; positive regulation of MAP kinase activity; positive regulation of membrane protein ectodomain proteolysis; positive regulation of mitosis; positive regulation of neuron apoptosis; positive regulation of NF-kappaB import into nucleus; positive regulation of NFAT protein import into nucleus; positive regulation of nitric oxide biosynthetic process; positive regulation of osteoclast differentiation; positive regulation of peptidyl-serine phosphorylation; positive regulation of phagocytosis; positive regulation of programmed cell death; positive regulation of protein amino acid phosphorylation; positive regulation of protein complex assembly; positive regulation of protein complex disassembly; positive regulation of protein kinase activity; positive regulation of protein kinase B signaling cascade; positive regulation of protein transport; positive regulation of smooth muscle cell proliferation; positive regulation of synaptic transmission; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; positive regulation of translational initiation by iron; protein import into nucleus, translocation; protein kinase B signaling cascade; receptor biosynthetic process; regulation of cell proliferation; regulation of I-kappaB kinase/NF-kappaB cascade; regulation of immunoglobulin secretion; regulation of insulin secretion; regulation of osteoclast differentiation; regulation of protein amino acid phosphorylation; regulation of protein secretion; response to glucocorticoid stimulus; response to lipopolysaccharide; response to organic substance; response to virus; sequestering of triacylglycerol; signal transduction; toll-like receptor 3 signaling pathway; tumor necrosis factor-mediated signaling pathway