Human IL-2 R gamma / CD132 Protein, His Tag, low endotoxin (MALS verified)

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Cat. No. / Size
Price
Qty
ILA-H52H5-100ug
$375.00
ILA-H52H5-1mg (500ug X 2)
$2695.00
ETA of in-stock products:2 business days

Product Details

  • Synonyms

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

  • Source

    Human IL-2 R gamma, His Tag (ILA-H52H5) is expressed from human 293 cells (HEK293). It contains AA Leu 23 - Asn 254 (Accession # P31785-1).

    Predicted N-terminus: Leu 23

    Request for sequence
  • Molecular Characterization

    IL-2 R gamma Structure

    Other Tags and Version Biotin & Other Labeled Version

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 29.3 kDa. The protein migrates as 55-65 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin

    Less than 0.01 EU per μg by the LAL method / rFC method.

  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process

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Performance Data

  • SDS-PAGE

    IL-2 R gamma SDS-PAGE

    Human IL-2 R gamma, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

  • SEC-MALS

    IL-2 R gamma SEC-MALS

    The purity of Human IL-2 R gamma, His Tag (Cat. No. ILA-H52H5) is more than 85% and the molecular weight of this protein is around 50-60 kDa verified by SEC-MALS.

    Report
  • Bioactivity-ELISA

     IL-2 R gamma ELISA

    Immobilized Human IL-2 Protein, Fc Tag (Cat. No. IL2-H5269) at 5 μg/mL (100 μL/well), add 50 μl/well of Human IL-2 R gamma, His Tag (Cat. No. ILA-H52H5) at increasing concentrations and then add Human IL-2 R beta, Fc Tag (Cat. No. ILB-H5253) at 5 μg/mL (50 μL/well). Detection was performed using HRP conjugated Anti-His Antibody (AY63), mAb (Acro, Cat. No. HIS-PLM535) with sensitivity of 0.32 μg/mL (QC tested).

    Protocol

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Background

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).

Recent Advances

 
Drug Development Progress
  • English Name:

    Interleukin-2 receptor subunit gamma

  • Category:

  • Approved Drugs:

    0 Details

  • Drugs in Clinical Trials:

    14 Details

  • Highest Development Stage:

    Phase 2 Clinical

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