Biotinylated Human IL-2 R gamma / CD132 Protein, His,Avitag™ (SPR verified)

Source : 

Biotinylated Human IL-2 R gamma, His,Avitag (ILG-H85E8) is expressed from Baculovirus-Insect cells. It contains AA Leu 23 - Asn 254 (Accession # P31785-1).

 

Molecule : IL-2 R gamma

 

Synonyms : IL2RG,CD132,CIDX,IMD4,P64,SCIDX,SCIDX1,gammaC

 

Format : Powder

 

Category : MABSol® Biotin Labeled Proteins

 

Accession : AAH14972.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 31.0 kDa

 

Characteristics :

This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag. The protein has a calculated MW of 31.0 kDa. The protein migrates as 40-50 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : PBS, pH7.4

 

Description :

IL-2R is a heterotrimeric protein binds and responds to the cytokine IL-2. Three distinct chains of IL-2R, termed as α, β and γ, which are non-covalently associated are identified. The α and β chains are involved in binding IL-2, while signal transduction following cytokine interaction is carried out by the γ chain, along with the β subunit. The α chain of the IL-2R can bind to the β chain before receptor interaction with IL-2. The γ chain alone has a very weak affinity for IL-2, but after the ligand is bound to the α/β heterodimer, the γ chain becomes recruited to the complex to form a very stable macromolecular quaternary ligand/receptor complex.
Interleukin-2 receptor subunit gamma (IL2RG), also known as cytokine receptor common subunit gamma, CD antigen CD132, gammaC, p64, which belongs to the type I cytokine receptor family or type 5 subfamily. IL2RG is located on the surface of immature blood-forming cells in bone marrow. Defects in IL2RG are the cause of severe combined immunodeficiency X-linked T-cell-negative/B-cell-positive/NK-cell-negative (XSCID).

 

References :

(1) Kondo M., et al., 1993, Science 262:1874-1877.
(2) Russell S.M., et al., 1993, Science 262:1880-1883.
(3) Noguchi M., et al., 1993, Science 262:1877-1880.