TNFR1 / CD120a / TNFRSF1A recombinant protein

Recombinant Mouse TNFR1 / CD120a / TNFRSF1A Protein (Fc tag)

Cat. Num. AAA2546950

• Gene Names: Tnfrsf1a; FPF; p55; TNF-R; TNFAR; TNFRI; Tnfr1; p55-R; CD120a; TNF-R1; TNFR60; Tnfr-2; TNF-R-I; TNF-R55; TNFRp55; TNF-alphaR1; TNFalpha-R1
• Purity: > 90 % as determined by SDS-PAGE
• Synonyms: TNFR1 / CD120a / TNFRSF1A; Recombinant Mouse TNFR1 / CD120a / TNFRSF1A Protein (Fc tag); Tnfrsf1; CD120a; FPF; TNF-R; TNF-R-I; TNF-R1; TNF-R55; TNF-alphaR1; TNFAR; TNFR60; TNFRI; TNFR1 / CD120a / TNFRSF1A recombinant protein

• Host: Human Cells
• Purity/Purification: > 90 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 454

• Application Notes: The secreted recombinant mouse TNFRSF1A/Fc is a disulfide-linked homodimer. The reduced monomer consists of 424 amino acids and has a predicted molecular mass of 47.4 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm TNFRSF1A/Fc monomer is approximately 55 kDa due to glycosylation.
• Predicted N Terminal: Leu 30
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for TNFR1 / CD120a / TNFRSF1A recombinant protein

Background: 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-kappaB, mediate apoptosis, and regulate inflammation processes.

Description: A DNA sequence encoding the mouse TNFRSF1A (NP_ 035739.2) extracellular domain (Met 1-Ala 212) was fused with the Fc region of human IgG1 at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 31560799
• NCBI GeneID: 21937
• NCBI Accession #: NP_035739.2
• NCBI GenBank Nucleotide #: NM_011609.4
• UniProt Accession #: P25118
• Molecular Weight: 50,130 Da
• NCBI Official Full Name: tumor necrosis factor receptor superfamily member 1A
• NCBI Official Synonym Full Names: tumor necrosis factor receptor superfamily, member 1a
• NCBI Official Symbol: Tnfrsf1a
• NCBI Official Synonym Symbols: FPF; p55; TNF-R; TNFAR; TNFRI; Tnfr1; p55-R; CD120a; TNF-R1; TNFR60; Tnfr-2; TNF-R-I; TNF-R55; TNFRp55; TNF-alphaR1; TNFalpha-R1
• NCBI Protein Information: tumor necrosis factor receptor superfamily member 1A
• UniProt Protein Name: Tumor necrosis factor receptor superfamily member 1A
• UniProt Gene Name: Tnfrsf1a
• UniProt Synonym Gene Names: Tnfr-1; Tnfr1; TNF-R1; TNF-RI; TNFR-I

NCBI Description

This gene encodes a member of the TNF receptor superfamily of proteins. The encoded receptor is found in membrane-bound and soluble forms that interact with membrane-bound and soluble forms, respectively, of its ligand, tumor necrosis factor alpha. Binding of membrane-bound tumor necrosis factor alpha to the membrane-bound receptor induces receptor trimerization and activation, which plays a role in cell survival, apoptosis, and inflammation. Proteolytic processing of the encoded receptor results in release of the soluble form of the receptor, which can interact with free tumor necrosis factor alpha to inhibit inflammation. Mice lacking a functional copy of this gene exhibit impaired immune function. [provided by RefSeq, Sep 2016]

Uniprot Description

TNF-R1: 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. 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. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; Receptor, cytokine

Chromosomal Location of Human Ortholog: 6 F3|6 59.32 cM

Cellular Component: axon; cell surface; cytosol; extracellular space; Golgi membrane; integral to plasma membrane; lipid raft; mitochondrion; nucleus; plasma membrane; protein complex; receptor complex; synapse

Molecular Function: protease binding; protein binding; protein complex binding; tumor necrosis factor binding; tumor necrosis factor receptor activity

Biological Process: cell surface receptor linked signal transduction; cytokine and chemokine mediated signaling pathway; defense response; defense response to bacterium; DNA damage response, signal transduction resulting in induction of apoptosis; immune response; induction of apoptosis via death domain receptors; inflammatory response; multicellular organismal development; negative regulation of apoptosis; negative regulation of inflammatory response; negative regulation of interleukin-6 production; positive regulation of angiogenesis; positive regulation of inflammatory response; positive regulation of neuron apoptosis; positive regulation of protein import into nucleus, translocation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tumor necrosis factor production; positive regulation of tyrosine phosphorylation of Stat1 protein; prostaglandin metabolic process; protein heterooligomerization; regulation of apoptosis; regulation of cell proliferation; response to lipopolysaccharide; tumor necrosis factor-mediated signaling pathway