CD1-CM122B-100μg / 询价
CD1-CM122B-500μg / 询价
CD1-CM122B-500μgx2 / 询价
Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Primary Amine Labeling)
Recombinant Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Primary Amine Labeling) is expressed from HEK293 with His tag at the C-Terminus. It contains Ala27-Asp239 [Accession | Q38J85].
The protein has a predicted MW of 25.6 kDa. Due to glycosylation, the protein migrates to 40-50 kDa based on Bis-Tris PAGE result.
>95% as determined by Bis-Tris PAGE
>90% as determined by HPLC
Less than 1 EU per μg by the LAL method.
Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
-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.
Biotinylated Cynomolgus IL-2 R beta on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Biotinylated Cynomolgus IL-2 R beta is greater than 90% as determined by SEC-HPLC.
Biotinylated 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 0.148 μM as determined in SPR assay (Biacore T200).
IL-2 R beta is a member of the cytokine receptor superfamily. Human IL-2 R beta cDNA encodes a 551 amino acid residue precursor Type I membrane protein with a 26 residue signal peptide, a 214 residue extracellular region, a 25 residue transmembrane region and a 286 residue cytoplasmic domain. Functional IL-2 receptors can exist in two affinity states on cell surfaces, the high affinity complex consisting of heterotrimers of the alpha, beta, and gamma chains, and the intermediate affinity complex comprising heterodimers of the beta and gamma chains.
CD122; IL-15 R beta; IL-2 R beta; IL-2R subunit beta; IL2RB; P70-75; p75; RP5-1170K4.6; IL-15 R β; IL-2 R β; IL-2R subunit β
(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).
