Biotinylated Cynomolgus IL-2 R gamma/CD132 Protein (Primary Amine Labeling)
Catalog No: IL2-CB003
- Species
- Cynomolgus
- Expression System
- HEK293
- Tag
- His
Product overview
Recombinant Biotinylated Cynomolgus IL-2 R gamma/CD132 Protein (Primary Amine Labeling) is expressed in HEK293 cells with a His tag at the C-terminus. It contains amino acid residues Leu23-Asn254 (UniProt accession: Q38JL2).
Product Details
- Molecular Aliases
- CD132; CIDX; IL-2 R gamma; IL2RG; IMD4; P64; SCIDX; SCIDX1; gammaC; IL2R gamma
- Protein Length
- Leu23-Asn254
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 28.2 kDa. Due to glycosylation, the protein migrates to 50-70 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display

Biotinylated Cynomolgus IL-2 R gamma on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
Background
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. Although IL-2 R gamma by itself does not bind IL-2 with any appreciable affinity, it is required for IL-2 receptor signaling.
References
- Smith K A. The structure of IL2 bound to the three chains of the IL2 receptor and how signaling occurs[J]. Medical Immunology, 2006, 5(1).
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