Anti-Mouse CD120a (TNFR1) (Clone 55R-593) – Purified in vivo PLATINUM™ Functional Grade
Pricing & Details
E. coli-expressed extracellular domain of the mouse TNFRI protein
≥ 5.0 mg/ml
<0.5 EU/mg as determined by the LAL method
≥98% monomer by analytical SEC
>95% by SDS Page
This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added.
Functional grade preclinical antibodies are manufactured in an animal free facility using only In vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s Purified Functional PLATINUM™ antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile.
Storage and Handling
Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
Next Day 2-8°C
Applications and Recommended Usage?
Quality Tested by Leinco
Other Applications Reported In Literature ?
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.
Clone 55R-593 recognizes mouse CD120a.
CD120a is constitutively expressed in most tissues.
CD120 can refer to two members of the tumor necrosis factor receptor superfamily- CD120a (TNFR1) or CD120b (TNFR2). CD120a is a 55kD Type I transmembrane protein receptor that binds both TNF-α and TNF-β (LT-α). In association with TRADD and RIP, the receptor crosslinking induced by TNF-α or TNF-β trimers is vital for signal transduction, leading to apoptosis, NF-B activation, increased expression of proinflammatory genes, tumor necrosis, and cell differentiation depending on cell type and differentiation state. CD120b is a 75 kD type I transmembrane protein that binds both TNF-α and TNF-β. In conjunction with TRAF1 and TRAF2, the receptor crosslinking induced by TNF-α or TNF-β trimers is critical for signal transduction that may lead to apoptosis, NF-kB activation, increased expression of proinflammatory genes, tumor necrosis, and cell differentiation depending on cell type and differentiation state. TNF-α is a 17.5 kD protein that mediates inflammation and immunity caused by the invasion of viruses, bacteria, and parasites by initiating a cascade of cytokines that increase vascular permeability, thus bringing macrophages and neutrophils to the site of infection. TNF-α secreted by the macrophage causes the blood to clot which provides containment of the infection. TNF-α binding to surface receptors brings about various biologic activities that include cytolysis and cytostasis of many tumor cell lines In vitro, hemorraghic necrosis of tumors In vivo, increased fibroblast proliferation, and enhanced chemotaxis and phagocytosis in neutrophils. TNF-β (LT-α) is a 25 kD protein that has a significant impact on the maintenance of the immune system including the development of secondary lymphoid organs. TNF-β has dual functions. It may function to prevent growth of cancer cells or it may facilitate the development of tumors. TNF-β is involved in the regulation of cell survival, proliferation, differentiation, and apoptosis and, if unregulated, can result in a constantly active signaling pathway, resulting in uncontrolled cellular growth and creation of tumors. Additionally, TNF-β is involved in innate immune regulation and has been shown to prevent tumor growth and obliterate cancerous cell lines.
TNF-α, LT-α (TNF-β)
Apoptosis, NF-κB activation, inflammation, tumor necrosis, cell differentiation
NCBI Gene Bank ID
References & Citations
1. Dana, R. et al. (2000) Arch Ophthalmol. 118: 1666
2. Donner, DB. et al. (2008) J Immunol. 181: 1288
3. Pasparakis, M. et al. (2008) Nat Immunol. 9: 1015