For immunohistology, flow cytometry and Western blotting, dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50. For functional studies, in vitro dilutions have to be optimized in user's experimental setting.
Restrictions
For Research Use only
Buffer
PBS, containing 0.1 % bovine serum albumin.
Storage
4 °C
Storage Comment
Product should be stored at 4 °C. Under recommended storage conditions, product is stable for one year.
Expiry Date
12 months
Grell, Wajant, Zimmermann, Scheurich: "The type 1 receptor (CD120a) is the high-affinity receptor for soluble tumor necrosis factor." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 2, pp. 570-5, (1998) (PubMed).
Thoma, Grell, Pfizenmaier, Scheurich: "Identification of a 60-kD tumor necrosis factor (TNF) receptor as the major signal transducing component in TNF responses." in: The Journal of experimental medicine, Vol. 172, Issue 4, pp. 1019-23, (1990) (PubMed).
Target
TNFRSF1A
(Tumor Necrosis Factor Receptor Superfamily, Member 1A (TNFRSF1A))
The monoclonal antibody H398 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-R1 and TNF-R2, which have both distinct and overlapping downstream signaling cascades. Induction of cytotoxicity and other functions are mediated largely via TNF-RI. TNF-R1 is equally well activated by both the 17 kDa soluble and 26 kDa membrane-bound form, whereas TNF-R2 is efficiently activated only by the membrane bound form of TNF-alpha. TNF-R1 signaling is initiated when trimeric TNF-alpha binds TNF-R1 receptors. Subsequent TNF-R1 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-R1-deficient mice indicate that TNF-R1 mediates most of the proliferation, pro-inflammatory, and apoptosis-activating pathways. Aliases CD120a, Tumor necrosis factor receptor superfamily member 1A, p55/p60, TNFR-1