Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Primary Amine Labeling) 3026

$525.00 – $1,750.00

Summary

Expression: HEK293
Binding assay: Yes (SPR)
Amino Acid Range: Ala27-Asp239

available size

Clear

SKU: 3026parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	C-His
purity	>95% as determined by Tris-Bis PAGE; >90% as determined by HPLC
background	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.
molecular weight	The protein has a predicted MW of 25.6 kDa. Due to glycosylation, the protein migrates to 40-50 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1 EU per μg by the LAL method.

Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Primary Amine Labeling) 3026

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
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.
Protein names Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (p70-75) (CD antigen CD122)
Gene names IL2RB,IL2RB
Protein family Type I cytokine receptor family, Type 4 subfamily
Mass 9541Da
Function Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (By similarity).
Subellular location Cell membrane ; Single-pass type I membrane protein. Cell surface .
Structure Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit. Interacts with SHB upon interleukin stimulation (By similarity).
Domain Th
Target Relevance information above includes information from UniProt accession: Q38J85
The UniProt Consortium

Data

SPR with Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Primary Ami

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).

HPLC of Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Primary Amin

The purity of Biotinylated Cynomolgus IL-2 R beta is greater than 90% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Cynomolgus IL-2 R beta/CD122 Protein (Prim

Biotinylated Cynomolgus IL-2 R beta on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.