IL2RG / CD132 Protein (His Tag) (Cytokine)

Interleukin 2 receptor, gamma Protein Datasheet

IL2RG / CD132 Protein Product Information

• Synonym: CD132, CIDX, IL-2RG, IMD4, P64, SCIDX, SCIDX1
• Protein Construction: A DNA sequence encoding the human IL2RG (P31785) extracellular domain (Met 1- Asn 254) was expressed, fused with a polyhistidine tag at the C-terminus.
• Source: Human
• Expression Host: Baculovirus-Insect cells

IL2RG / CD132 Protein QC Testing

• Purity: > 97 % as determined by SDS-PAGE.
• Bio-activity: Measured by its ability to bind biotinylated recombinant rat IL2 in a functional ELISA.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Leu 23
• Molecular Mass: The recombinant human IL2RG consists of 242 amino acids and predicts a molecular mass of 28.8 kDa. The apparent molecular mass of rhIL2RG is approximately 43 kDa in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: IL2RG / CD132 protein

IL2RG / CD132 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

IL2RG / CD132 Protein Description

The interleukin 2 receptor (IL-2R) is a heterotrimeric protein expressed on the surface of certain immune cells, such as lymphocytes, which 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 which are members of the type I cytokine receptor family. 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. It is proposed that the γ chain is common to the IL2, IL4, IL7, IL21 and probably also the IL13 receptors.

References

1. Robb RJ. et al., 1981, J Exp Med. 154 (5): 1455-1474.
2. Leonard WJ. et al., 1982, Nature. 300 (5889): 267-269.
3. Sharon M. et al., 1986, Science. 234 (4778): 859-863.
4. Tsudo M. et al., 1987, Proc Natl Acad Sci.  84 (12): 4215-4218.
5. Takeshita T. et al., 1992, J Immunol. 148 (7): 2154-2158.
6. Johnson K. et al., 1994, Eur Cytokine Netw. 5 (1): 23-34.