Cynomolgus IL-2 R beta/CD122 Protein (CD1-CM122)

  • Express System: Expi293
  • Product Tag: C-His
  • Purity: > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
  • Activity: The affinity constant of 0.17 μM as determined in SPR assay (Biacore T200). See testing image for detail.
  • Exact Sequence: Ala27-Asp239

Catalog: CD1-CM122

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Product Description Recombinant Cynomolgus IL-2 R beta/CD122 Protein is expressed from Expi293 with His tag at the C-terminal.It contains Ala27-Asp239.
Product Category Recombinant Protein
Target IL-2 R beta/CD122
Synonyms CD122; IL-15 R beta; IL-2 R beta; IL-2R subunit beta; IL2RB; P70-75; p75; RP5-1170K4.6
Gene/Protein ID Q38J85
Species Cynomolgus
Exact Sequence Ala27-Asp239
Molecular Weight The protein has a predicted MW of 25.6 kDa. Due to glycosylation, the protein migrates to 38-45 kDa based on Tris-Bis PAGE result.
Activity The affinity constant of 0.17 μM as determined in SPR assay (Biacore T200). See testing image for detail.
Product Tag C-His
Express System Expi293
Purity > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
Endotoxin Less than 1EU per μg by the LAL method.
Form Lyophilized
Shipping Shipped at ambient temperature.
Formulation Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 5% trehalose is added as protectant before lyophilization.
Reconstitution Centrifuge tubes before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Stability And Storage Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Cynomolgus IL-2 R beta, His Tag captured on CM5 Chip via anti-his antibody can bind Human IL-2, No Tag with an affinity constant of 0.17 μM as determined in SPR assay (Biacore T200).
The purity of Cynomolgus IL-2 R beta is greater than 95% as determined by SEC-HPLC.
Cynomolgus IL-2 R beta on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

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