Recombinant Human gp130 His-tag Avi-tag Protein, CF

Glycoprotein 130 (gp130; also known as IL-6 signal transducer, IL-6 receptor beta, oncostatin-M alpha subunit) is a ubiquitously expressed, 130 kDa type I transmembrane glycoprotein and member of the type II subfamily, type I cytokine receptor family. Functionally, it is responsible for transduction of the IL-6 signal across the plasma membrane (1). Human gp130 is synthesized as a 918 amino acid (aa) precursor with a 22 aa signal sequence, a 597 aa extracellular domain (ECD), a 22 aa transmembrane region, and a 277 aa cytoplasmic tail. The ECD also contains an N terminal immunoglobulin (Ig)-like C2-type domain, followed by the cytokine receptor homology region (CHR) which is made up of two fibronectin type III-like domains and a WSXWS motif, and three additional fibronectin type III-like domains (2). The domains in the CHR are the structural hallmarks of the hematopoietic cytokine receptor family (1-2). The ECD of human gp130 shares 73% and 75% aa sequence identity with that of mouse and rat gp130, respectively. Gp130 serves as the signal transducing receptor subunit for the IL-6-type cytokines consisting of interleukin (IL)‑6, IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF), new neurotrophin factor-1 (NNT-1), IL-27, cardiotrophin-1 (CT-1), and cardiotrophin like cytokine (CLC) (2 - 5). These cytokines are involved in a variety of functions including the modulation of inflammatory and immune responses, heart development, fertility, and many other activities (2). Our Avi-tag Biotinylated human gp130 His-tag features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.