Human gp130 Protein Dimer, His-Avi Tag

Cytokine Receptor

Product Code: CSP-24081-03
Expression Host: HEK293T
Verified Applications: ELISA for gp130-specific antibody and interleukin-6 (IL-6) ligand protein binding assays.
Suggested Applications: ELISA for gp130-specific antibody and interleukin-6 (IL-6) ligand protein binding assays. SPR & BLI for gp130-specific antibody and IL-6 protein binding assays. Animal immunization, RUO.
Purity: Greater than 90% dimer form as determined by SDS-PAGE under non-reducing condition
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Formulation: 0.22μm filtered PBS, pH 7.4
Shipping: Frozen Dry Ice
Storage: -80’C
Human glycoprotein 130 (gp130), is a transmembrane protein and a member of the class of tall cytokine receptors. The recombinant gp130 dimer protein (CSP-24081-03) is a cis-homodimer (cis-dimer) and contains a gp130 extracellular domain (UniProt# P40189, amino acids Glu23-Glu619) fused with a proprietary dimer motif followed by a tandem His-Avi tag at the C-terminus. This dimeric protein is expressed in HEK293 cells. The recombinant human gp130 dimer protein is bioactive and can bind to interleukin-6 (IL-6). It also binds gp130-specific antibodies. This gp130 dimer can be used as an antigen for in vitro assays and antibody screening, and as an immunogen for immunization to generate antibodies targeting more conformational epitopes.
Protein Name: gp130
UniProt #: AA: P40189
Predicted Molecular Weight: 156 kDa
SDS PAGE Molecular Weight: The migration range of the dimer protein with glycosylation under non-reducing conditions is >190 kDa on SDS PAGE.
Protein Construct: Gp130 dimer protein contains a gp130 extracellular domainfused with a proprietary dimer motif followed by a tandem His-Avi tag at the C-terminus.

Background

Human glycoprotein 130 (gp130), is a transmembrane protein and a member of the class of tall cytokine receptors. Gp130 is also known as Interleukin 6 Cytokine Family Signal Transducer (IL6ST), Cluster of Differentiation 130 (CD130), CDW130, and Interleukin-6 Receptor Subunit Beta (IL6Rb). Gp130 serves as a shared signal transducing subunit of the receptor complexes for at least nine human cytokines including: interleukin-6 (IL-6), interleukin-11 (IL-11), interleukin-27 (IL-27), leukemia inhibitory factor (LIF), ciliary neurotrophic factor (CNTF), oncostatin M (OSM), cardiotrophin-1 (CT-1), cardiotrophin-like cytokine (CLC/CLCF-1), and neuropoietin (NP) that mediate highly diverse biological processes. Gp130 can form homodimers and heterodimers with other cytokine receptors (i.e., IL-6 receptor alpha (IL-6Ra)) in response to cytokine binding. The homodimerization or heterodimerization of gp130 is key to initiating intracellular signaling pathways, resulting in the activation of gp130-associated JAKs (JAK1, JAK2, and TYK2). The extracellular domain of gp130 includes an N-terminal immunoglobulin-like (Ig-like) domain (D1), a cytokine-binding homology region (CHR, D2D3), and three membrane-proximal fibronectin type III domains (FNIII, D4 to D6) followed by a transmembrane domain and cytoplasmic domain. It has been found that dysregulation of gp130 expression and signaling mediates progression for multiple types of cancer and autoimmune diseases. Inhibition of gp130 activity offers a potential and promising approach to cancer and autoimmune disease therapy.