Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Additional Information | Biotinylated |
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Details of Functionality | Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human gp130 His-tag Avi-tag is captured on a Streptavidin Coated Plate
(Catalog #
CP004), it binds to Recombinant Human IL-6
(Catalog #
7270-IL) in the presence of Recombinant Human IL-6R alpha
(Catalog # 227-SR). The ED50 for this binding is 0.800-4.80 ng/mL. |
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Source | Human embryonic kidney cell, HEK293-derived human gp130 protein
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Accession # | |||||||
N-terminal Sequence | Glu23 |
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Structure / Form | Biotinylated via Avi-tag |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 70 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 93-103 kDa, under reducing conditions. |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 500 μg/mL in PBS. |
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.
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