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E Tag is a commonly used epitope tag engineered onto the N- or C- terminus of a protein of interest so that the tagged protein can be analyzed and visualized.$nBecause of the small size of the epitope, it is unlikely to alter the activity of the cloned sequence.

UCPs facilitate the transfer of anions from the inner to the outer mitochondrial membrane and the return transfer of protons from the outer to the inner mitochondrial membrane. They also reduce the mitochondrial membrane potential in mammalian cells. UCP2 gene is expressed in many tissues, with the greatest expression in skeletal muscle. UCP2 is thought to play a role in non shivering thermogenesis, obesity and diabetes.

TLR1 is a member of the Toll like receptor (TLR) family which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expr

This locus encodes the transforming growth factor (TGF)-beta type III receptor. The encoded receptor is a membrane proteoglycan that often functions as a co-receptor with other TGF-beta receptor superfamily members. Ectodomain shedding produces soluble TGFBR3, which may inhibit TGFB signaling. Decreased expression of this receptor has been observed in various cancers. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[provided by RefSeq, Se

This protein is a transcription factor that negatively regulates other myogenic family proteins. Studies of the mouse homolog, I-mf, show that it interferes with myogenic factor function by masking nuclear localization signals and preventing DNA binding. Knockout mouse studies show defects in the formation of vertebrae and ribs that also involve cartilage formation in these structures. [provided by RefSeq, Jul 2008]

Fibrinogen is the main protein of blood coagulation system. It is a large protein and it consists of two identical subunits that contain three polypeptide chains: alpha, beta and gamma. All chains are connected with each other by a number of disulfide bonds. Fibrinopeptides A (1 to 16 amino acids) and B (1 to 17 amino acids) are released by thrombin from the N terminal parts of alpha and beta chains, respectively. In this way fibrinogen is converted into fibrin, which by means of polymeriza