IL-2 R beta/IL-2 R gamma Products

Description

Interleukin-2 receptor subunit beta (IL-2 RB), also known as high affinity IL-2 receptor subunit beta, interleukin-15 receptor subunit beta, p70-75 (p75), and CD122, is a member of the cytokine receptor superfamily that plays a role in T cell-mediated immune responses (1, 2). Human IL-2 RB consists of an extracellular domain (ECD) containing a fibronectin type III domain and a WSXWS motif, a type I transmembrane domain, and a cytoplasmic tail. The gamma chain of the high affinity functional human IL-2 receptor complex belongs to the hematopoietin receptor family. IL-2 R gamma is a 369 amino acid residue protein consisting of a 22 residue signal sequence, a 232 residue extracellular domain, a 29 residue transmembrane domain and an 86 residue cytoplasmic domain. Functional IL-2 receptors can exist in two affinity states on cell surfaces: the high affinity complex consisting of heterotrimers of the alpha, beta, and gamma chains and the intermediate affinity complex comprising heterodimers of the beta and gamma chains (2, 3). Individual beta chains and alpha chains exhibit low affinity IL-2 binding and the gamma chain alone does not bind IL-2. In addition to their involvement in IL-2 mediated signal transduction, both the beta chain and gamma chain have been shown to be required for IL-15 mediated signaling (4). 

Bioinformatics

Product By Gene ID	3560
Alternate Names	CD122 CD132 CIDX High affinity IL-2 receptor subunit beta IL15RB IL-2 R beta/IL-2 R gamma IL-2 receptor subunit beta IL-2RG IMD4 IMD63 P64 SCIDX