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TNFR1/TNFRSF1A/CD120a  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: Human Cells  
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10872-H03H-50
10872-H03H-100
50 µg 
100 µg 
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Description: Active  
Expression host: Human Cells  
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10872-H08H-50
10872-H08H-100
50 µg 
100 µg 
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Description: Active  
Expression host: Human Cells  
  • Slide 1
50496-M08H-50
50496-M08H-100
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100 µg 
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Expression host: Human Cells  
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50496-M02H-50
50496-M02H-100
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100 µg 
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Expression host: Human Cells  
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80181-R02H-50
80181-R02H-100
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100 µg 
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Description: Active  
Expression host: Human Cells  
  • Slide 1
80181-R08H-5
80181-R08H-20
80181-R08H-100
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20 µg 
100 µg 
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TNFR1/TNFRSF1A/CD120a Related Pathways

TNFR1/TNFRSF1A/CD120a Related Protein, Antibody, cDNA Gene, and ELISA Kits

TNFR1/TNFRSF1A/CD120a Related Protein, Antibody, cDNA Gene, and ELISA Kits

TNFR1/TNFRSF1A/CD120a Summary & Protein Information

TNFR1/TNFRSF1A/CD120a Background

Gene Summary: The protein encoded by this gene is 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.
General information above from NCBI
Subunit structure: Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with HCV core protein. Interacts with human cytomegalovirus/HHV-5 protein UL138.
Domain: The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.
Both the cytoplasmic membrane-proximal region and the C- terminal region containing the death domain are involved in the interaction with TRPC4AP (By similarity).
Subcellular 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.
Isoform 4: Secreted. Note=Lacks a Golgi- retention motif, is not membrane bound and therefore is secreted.
Post-translational: The soluble form is produced from the membrane form by proteolytic processing.
Involvement in disease: Familial hibernian fever (FHF) [MIM:142680]: A hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases. Note=The disease is caused by mutations affecting the gene represented in this entry.
Multiple sclerosis 5 (MS5) [MIM:614810]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry. An intronic mutation affecting alternative splicing and skipping of exon 6 directs increased expression of isoform 4 a transcript encoding a C- terminally truncated protein which is secreted and may function as a TNF antagonist.
Sequence similarity: Contains 1 death domain.
Contains 4 TNFR-Cys repeats.
General information above from UniProt

The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD120a (cluste of differentiation 120a), also known as TNFR1 / TNFRSF1A, is a member of CD family, tumor necrosis factor receptor superfamily. CD120a is one of the most primary receptors for the tumor necrosis factor-alpha. It has been shown to be localized to both plasma membrane lipid rafts and the trans golgi complex with the help of the death domain (DD). CD120a can activate the transcription factor NF-κB, mediate apoptosis, and regulate inflammation processes.

TNFR1/TNFRSF1A/CD120a Alternative Name

TNFR1/TNFRSF1A/CD120a Related Studies

  • Zola H, et al. (2007) CD molecules 2006-human cell differentiation molecules. J Immunol Methods. 318 (1-2): 1-5.
  • Ho IC, et al. (2009) GATA3 and the T-cell lineage: essential functions before and after T-helper-2-cell differentiation. Nat Rev Immunol. 9 (2): 125-35.
  • Matesanz-Isabel J, et al. (2011) New B-cell CD molecules. Immunology Letters.134 (2): 104-12.
  • Cottin V, et al. (2002) Restricted localization of the TNF receptor CD120a to lipid rafts: a novel role for the death domain. The journal of immunology. 168: 4095-102.
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