Human gp130/CD130 recombinant protein

Human gp130/CD130 recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Glycoprotein 130 (also known as gp130, IL6ST, IL6-beta or CD130) is a transmembrane protein which is the founding member of the class of all cytokine receptors. CD130/gp130 is a signal transducer shared by many cytokines, including interleukin 6 (IL6), ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF), and Oncostatin M (OSM). CD130/gp130 functions as a part of the cytokine receptor complex. The activation of this protein is dependent upon the binding of cytokines to their receptors. CD130/gp130 plays a critical role in regulating myocyte apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been described. A related pseudogene has been identified on chromosome 17. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. CD130/gp130 binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. CD130/gp130 may have a role in embryonic development. The type I OSM receptor is capable of transducing OSM-specific signaling events.

Interleukin-6 receptor subunit beta

IL6ST; CDW130; GP130-RAPS; CD130; 5133400A03RIK; GP130; AA389424; D13ERTD699E; IL6R-BETA; IL-6RB; BB405851

Q17RA0

IL6ST

Human Cells

A DNA sequence encoding the human IL6RB (NP_002175.2)(Met1-Ile618) was expressed with six amino acids (ENLYFQ) at the C-terminus.

Human

The recombinant human IL6RB consists of 603 amino acids and predicts a molecular mass of 68.6 KDa. It migrates as an approximately 69-99 KDa band in SDS-PAGE under reducing conditions due to glycosylation.

> 90 % as determined by SDS-PAGE