Rat TNFRSF11A Protein (Fc Tag)

TNFRSF11A

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Catalog Number	P80160-R02H
Organism Species	Rat
Host	Human Cells
Synonyms	TNFRSF11A
Molecular Weight	The recombinant rat TNFRSF11A/Fc is a disulfide-linked homodimer. The reduced monomer comprises 424 amino acids and has a predicted molecular mass of 47.1 kDa. The apparent molecular mass of the protein is approximately 61 kDa in SDS-PAGE under reducing conditions.
predicted N	Val 31
SDS-PAGE
Purity	> 80 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the rat TNFRSF11A (Met1-Pro213) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Bio-activity
Research Area	Immunology |Signal Transduction |Cytoskeleton / ECM |Extracellular Matrix |Structures |Bone |
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	TNFRSF11A is a member of the TNF-receptor superfamily. In mouse, it is also known as CD265. TNFRSF11A contains 4 TNFR-Cys repeats and is widely expressed with high levels in skeletal muscle, thymus, liver, colon, small intestine and adrenal gland. It is an essential mediator for osteoclast and lymph node development. TNFRSF11A and its ligand are important regulators of the interaction between T cells and dendritic cells. It can interact with various TRAF family proteins, through which this receptor induces the activation of NF-kappa B and MAPK8/JNK. Defects in TNFRSF11A can cause familial expansile osteolysis (FEO). FEO is a rare autosomal dominant bone disorder characterized by focal areas of increased bone remodeling. Defects in TNFRSF11A also can cause Paget disease of bone type 2 (PDB2). PDB2 is a bone-remodeling disorder with clinical similarities to FEO. Defects in TNFRSF11A are the cause of osteopetrosis autosomal recessive type 7 which characterized by abnormally dense bone, due to defective resorption of immature bone.
Reference	Darnay B G, et al. (1998) Characterization of the intracellular domain of receptor activator of NF-kappaB (RANK). Interaction with tumor necrosis factor receptor-associated factors and activation of NF-kappab and c-Jun N-terminal kinase. J Biol Chem. 273(32):20551-5. Darnay B G, et al. (1999) Activation of NF-kappaB by RANK requires tumor necrosis factor receptor-associated factor (TRAF) 6 and NF-kappaB-inducing kinase. Identification of a novel TRAF6 interaction motif. J Biol Chem. 274(12):7724-31. Galibert L, et al. (1998) The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-kappaB, a member of the TNFR superfamily. J Biol Chem. 273(51):34120-7.