tnf-r1

Tumour necrosis factor alpha (TNF-α) is a pleiotropic cytokine with both injurious and protective functions, which are thought to diverge at the level of its two cell surface receptors, TNFR1 and TNFR2. In the setting of acute injury, selective inhibition of TNFR1 is predicted to attenuate the cell death and inflammation associated with TNF-α, while sparing or potentiating the protective effects of TNFR2 signalling.

TNFR1 CD120a TNFRSF1A Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 21.8 kDa and the accession number is P25118.

TNFR1 CD120a TNFRSF1A Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 47.4 kDa and the accession number is P25118.

Tumor necrosis factor receptor superfamily member 1A (Tnfrsf1a) is a member of the tumor necrosis factor receptor superfamily. Tnfrsf1a is one of the major receptors for the tumor necrosis factor-alpha. It can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4 SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor. Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome

TNFR1 CD120a TNFRSF1A Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 22.7 kDa and the accession number is P19438-1.

TNFR2 CD120b TNFR1B Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 52.3 kDa and the accession number is P25119.

TNFR2 CD120b TNFR1B Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 26.8 kDa and the accession number is P25119.

TNFR1 CD120a TNFRSF1A Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 48 kDa and the accession number is P19438-1.

TNFR1 CD120a TNFRSF1A Protein, Human, Recombinant (Avi & His), Biotinylated is expressed in HEK293 Cells. The accession number is P19438-1.

Expression system: E. coli
Length: 1-656, Full Length
Activity: Not Tested

Tumor necrosis factor receptor superfamily member 10A (TNFRSF10A) is also known as TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1), Death receptor 4 (DR4), CD261 and APO2, which belongs to TNF superfamily. TNFRSF10A DR4 is widely expressed and high levels are found in spleen, peripheral blood leukocytes, small intestine and thymus, but also in K-562 erythroleukemia cells, MCF-7 breast carcinoma cells and activated T-cells. APO2 TNFRSF10A is receptor for the cytotoxic ligand TNFSF10 TRAIL. This receptor is activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF1 TRAIL), and thus transduces cell death signal and induces cell apoptosis. TRAIL R1 can promote the activation of NF-kappa-B. TRAIL R1 CD261 TNFRSF1A induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types.

Expression system: E. coli
Length: 78-235, Partial
Activity: Not Tested

The cellular inhibitor of apoptosis protein-1 (cIAP1) is a member of the Inhibitor of Apoptosis family proteins are (IAP) whose members are characterized by a novel domain of about 70 amino acids termed baculoviral IAP repeats (BIRs). The BIR domains of cIAP1 and cIAP2 bind to caspases, the key effector proteases of apoptosis. The IAP protein family which can enhance cell survival are crucial regulators of programmed cell death. Both cIAP1 and cIAP2 are the E3 ubiquitin protein isopeptide ligases for Smac, taking part in promoting cancer survival through functioning as E3 ubiquitin ligases. Removal of cIAP1 by genetic deletion may result in NF-κB signaling activation that induces TNFα production and in killing sensitive tumor cells through enhanced TNF-R1 death-receptor signaling and caspase 8 activation. The substrate-dependent E3 activity of cIAPs is mediated by their RING domains and is dependent on the specific interactions between cIAPs and Smac. cIAP1 and cIAP2 are also reported to be regulators of NF-kB activation upon TNFαtreatment.