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The monoclonal antibody HM104 recognizes the extracellular part of the Tumor Necrosis Factor Receptor type I (TNF-RI) of the membrane-bound as well as the soluble receptor. TNF-RI (~55-60 kDa) is present on most cell types and is considered to play a prominent role in cell stimulation by TNF-alpha. TNF-alpha activates inflammatory responses, induces apoptosis, regulates cellular proliferation, and may even promote cancer progression. The effects of TNF-alpha are mediated by TNF-RI and TNF-RII, which have both distinct and overlapping downstream signaling cascades. Induction of cytotoxicity and other functions are mediated largely via TNF-RI. TNF-RI is equally well activated by both the 17 kDa soluble and 26 kDa membrane-bound form, whereas TNF-RII is efficiently activated only by the membrane bound form of TNF-alpha. TNF-RI signaling is initiated when trimeric TNF-alpha binds TNF-RI receptors. Subsequent TNF-RI trimerization promotes the recruitment of a proximal signaling complex composed of TNF Receptor Associated protein with a Death Domain (TRADD), Receptor Interacting Protein (RIP), cellular Inhibitor of Apoptosis Protein 1 (cIAP1), TNF Receptor Associated Factor 2 (TRAF2), and likely TRAF5. Studies with TNF-RI-deficient mice indicate that TNF-RI mediates most of the proliferation, pro-inflammatory, and apoptosis-activating pathways.
TNFR1 (Tumor necrosis factor receptor 1) belongs to the tumor necrosis factor superfamily, and is one of the major TNF-alpha receptors. TNFR1 plays an important role in mediating, in cytokine mediated signaling, positive regulation of the NF-Kb pathway, positive regulation of angiogenesis, and negative regulation of gene expression. The extracellular domain of TNFR1 is also released into the circulatory system as soluble TNFR1 (sTNFR1). In humans, the TNFR1 gene is located on chromosome 12. Anti-apoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with TNFR1, and thus play regulatory roles in the signal transduction mediated by the receptor. Germline mutations of the extracellular domains of TNFR1 were found to be associated with the autosomal dominant periodic fever syndrome, and the impaired receptor clearance is thought to be a mechanism of the disease.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: CD120a; CD120a antigen; MGC19588; n-smase activation assoc. factor; p55; p60; p62; p63; sCD120a; soluble CD120a; soluble TNFR1; sTNF RI; sTNFR I; sTNFR1; sTNFRI; TNF receptor alpha chain; TNF-alpha-R1; TNF-R1; TNF-RI; TNFR; TNFR I; TNFR-I; Tumor necrosis factor receptor; Tumor necrosis factor receptor 1; Tumor necrosis factor receptor superfamily member 1A; Tumor necrosis factor receptor type I
基因别名: CD120a; FPF; p55; p55-R; TNF-alphaR1; TNF-R; TNF-R-I; TNF-R1; TNF-R55; TNFalpha-R1; TNFAR; Tnfr-1; Tnfr-2; Tnfr1; TNFR60; TNFRI; TNFRp55; Tnfrsf1a
UniProt ID: (Mouse) P25118
Entrez Gene ID: (Mouse) 21937