Human TNF-alpha組換え体(リコンビナント)タンパク質 | Recombinant Human TNF-alpha

R&D Systems社製の高品質なHuman TNF-alphaの組換え体タンパク質(Recombinant Human TNF-alpha)です。

※本製品は研究用です。研究用以外には使用できません。

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R&D Systems社組換え体タンパク質製品では通常ウシ血清アルブミン(BSA)をキャリアタンパク質として加えています。キャリアタンパク質を加えることで組換え体タンパク質の安定性が高まり、使用期限が長くなります。また、より濃度の低い溶液での保管も可能となります。CF製品はBSAが含まれない製品となります。一般的に細胞培養や、ELISAのスタンダードにはBSA含有製品を推奨しています。CF製品はBSAが影響してしまうアプリケーションに推奨されます。

Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF1A, 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). This recombinant protein contains an N-terminal insertion and a Leu233Phe substitution which have been shown to increase the bioactivity of TNF-alpha in vitro and in vivo (16).