货号 | AFL210-02M |
别名 | APC1 protein; Cachectin; Cachetin; DIF; TNF; TNF, monocyte-derived; tnfa; tnf-a; TNF-alphacachectin; TNFATNF, macrophage-derived; TNFSF1A; TNFSF2; TNFSF2TNF superfamily, member 2; tumor necrosis factor (TNF superfamily, member 2); tumor necrosis factor alpha; Tumor necrosis factor ligand superfamily member 2; tumor necrosis factor; tumor necrosis factor-alpha | 全称 | Tumor Necrosis Factor alpha |
反应种属 | Human |
来源 | E. coli-derived Val77-Leu233, with and without an N-terminal Met Produced using non-animal reagents in an animal-free laboratory. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 7124 (Human); 21926 (Mouse); 24835 (Rat); 397086 (Porcine); 280943 (Bovine); 403922 (Canine); 100033834 (Equine); 493755 (Feline); 100009088 (Rabbit) |
内毒素水平 | <0.10 EU per 1 μg of the protein by the LAL method. |
生物活性 | Measured in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. Matthews, N. and M.L. Neale (1987) in Lymphokines and Interferons, A Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 221. The ED50 for this effect is typically 25-100 pg/mL. The specific activity of Recombinant Human TNF-alpha is approximately 7.6 x 104 IU/μg, which is calibrated against human TNF-alpha WHO International Standard (NIBSC code: 88/786). |
溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
背景 | 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). Human TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 177 aa extracellular domain (ECD) (3). Within the ECD, human TNF-alpha shares 97% aa sequence identity with rhesus and 71%-92% with bovine, canine, cotton rat, equine, feline, mouse, porcine, and rat 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). |
Accession # | P01375 |
运输条件 | Blue Ice |
N-terminal Sequence Analysis | Met & Val77 |
预期分子量 | 17.5 kDa |
SDS-PAGE | 17 kDa, reducing conditions |
存放说明 | -20℃ |
纯度 | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
参考文献 |
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