Recombinant Human Common gamma Chain Avi-tag His Protein, CF

Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human Common gamma Chain Avi-tag His-tag (Catalog # AVI384) binds to Recombinant Human CD25/IL-2R alpha Protein (223-2A), Recombinant Human IL-2R beta Protein (224-2B) and Recombinant Human IL-2 Protein (202-IL) with an ED50 of 0.100-1.00 μg/mL.

2 μg/lane of Biotinylated Recombinant Human Common gamma Chain Avi-tag His-tag Protein (Catalog # AVI384) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 60‑67 kDa, under reducing conditions.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Common gamma Chain Avi-tag His Protein, CF Summary

• Additional Information: His-tag
• Details of Functionality: Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human Common gamma Chain Avi-tag His-tag binds to Recombinant Human CD25/IL-2R alpha Protein (Catalog # 223-2A), Recombinant Human IL-2R beta Protein (Catalog # 224-2B), and Recombinant Human IL-2 Protein (Catalog # 202-IL) with an ED₅₀ of 0.100-1.00 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human Common gamma Chain/IL-2 R gamma protein
  Leu23-Asn254 with a C-terminal Avi-tag & 6-His tag
• Accession #: P31785.1
• N-terminal Sequence: Leu23
• Structure / Form: Biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 32 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 60-67 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Common gamma Chain Avi-tag His Protein, CF

• CD132 antigen
• CD132
• CIDX
• combined immunodeficiency, X-linked
• common cytokine receptor gamma chain
• Common gamma Chain
• common gamma-chain
• cytokine receptor common subunit gamma
• gamma(c)
• IL-2 R gamma
• IL-2 receptor subunit gamma
• IL2R gamma
• IL-2R subunit gamma
• IL2RG
• IL-2RG
• IMD4
• interleukin 2 receptor, gamma
• Interleukin-2 receptor subunit gamma
• p64
• SCIDX
• SCIDX1
• severe combined immunodeficiency

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. Besides IL-2, the gamma  chain has been shown to be a component of the functional receptor complexes for IL-4, IL-7, IL-9 and IL-15. It has been proposed that IL-2 R gamma be designated the common gamma chain ( gamma _c). The site of molecular defects in X-linked SCID (severe combined immunodeficiency) has now been mapped to the IL-2 R gamma gene. Our Avi-tag Biotinylated IL-2 R gamma  features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide.  Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

1. Minami, Y. et al. (1993) Annu. Rev. Immunol. 11:245.
2. Noguchi, M. et al. (1993) Science 262:1877.

Bioinformatics

• Uniprot:
  • P31785.1()