PROVETOP

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

Bis-Tris PAGE
IL2-CB003 Bis-Tris-PAGE-white result

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

  1. 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).

Have questions about this product?

Our technical team can help with product selection, application questions and order support.

Contact Technical Support