|Other Names||Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tumor necrosis factor receptor superfamily member 1A, membrane form, Tumor necrosis factor-binding protein 1, TBPI, TNFRSF1A, TNFAR, TNFR1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP3274a was selected from the region of human Phospho-TNFR-S274. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate- specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein Golgi apparatus membrane; Single- pass type I membrane protein Secreted. Note=A secreted form is produced through proteolytic processing|
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Provided below are standard protocols that you may find useful for product applications.
A member of the TNF-receptor superfamily, this protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate NF-kappaB, 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 autosomal dominant periodic fever syndrome. The impaired receptor clearance is thought to be a mechanism of the disease.
Kuo, N.W., et al., Invest. Ophthalmol. Vis. Sci. 46(5):1565-1571 (2005).Siebert, S., et al., Arthritis Rheum. 52(4):1287-1292 (2005).Spahr, L., et al., J. Hepatol. 41(2):229-234 (2004).Wang, W.H., et al., Mol. Cell. Biol. 24(23):10352-10365 (2004).Tashiro, H., et al., Transpl. Int. 17(10):626-633 (2004).
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