CD130 / GP130 Mouse Monoclonal Antibody [B11-B9-A8]

Function

Glycoprotein 130 (also known as gp130, IL6ST, IL6R-beta or CD130) is a transmembrane protein which is the founding member of the class of tall cytokine receptors. It forms one subunit of the type I cytokine receptor within the IL-6 receptor family. It is often referred to as the common gp130 subunit, and is important for signal transduction following cytokine engagement. As with other type I cytokine receptors, gp130 possesses a WSXWS amino acid motif that ensures correct protein folding and ligand binding. It interacts with Janus kinases to elicit an intracellular signal following receptor interaction with its ligand. Structurally, gp130 is composed of five fibronectin type-III domains and one immunoglobulin-like C2-type (immunoglobulin-like) domain in its extracellular portion.

Background References

1. Schutt A et al. gp130 activation is regulated by D2-D3 interdomain connectivity. Biochem. J. 450:487-496 (2013).

2. Waetzig GH et al. N-linked glycosylation is essential for the stability but not the signaling function of the interleukin-6 signal transducer glycoprotein 130. J. Biol. Chem. 285:1781-1789 (2010).

Sequence Similarity

Belongs to the type I cytokine receptor family. Type 2 subfamily.

Tissue Specificity

Found in all the tissues and cell lines examined. Expression not restricted to IL6 responsive cells. Expressed in blood serum (at protein level).

Post-translational Modification

Phosphorylation of Ser-782 down-regulates cell surface expression.; Heavily N-glycosylated. Glycosylation is required for protein stability and localization in plasma membrane but not for ligand binding.

Subcellular Location

Cell membrane.

UNIPROT

SwissProt: P40189 Human

SwissProt: Q00560 Mouse

Synonyms