It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50. Product should be stored at 4 °C. Under recommended storage conditions, product is stable for one
Restrictions
For Research Use only
Buffer
PBS, containing 0.1 % bovine serum albumin and 0.02 % sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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
Ghezzi, Cerami: "Tumor necrosis factor as a pharmacological target." in: Methods in molecular medicine, Vol. 98, pp. 1-8, (2004) (PubMed).
Mennini, Bigini, Cagnotto, Carvelli, Di Nunno, Fumagalli, Tortarolo, Buurman, Ghezzi, Bendotti: "Glial activation and TNFR-I upregulation precedes motor dysfunction in the spinal cord of mnd mice." in: Cytokine, Vol. 25, Issue 3, pp. 127-35, (2003) (PubMed).
Target
TNFRSF1A
(Tumor Necrosis Factor Receptor Superfamily, Member 1A (TNFRSF1A))
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-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. CD120a, Tumor necrosis factor receptor superfamily member 1A, p55/p60, TNFR-1 Aliases Rat IgG2a