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Cynomolgus IL-2 R beta/CD122 Protein 4627

$375.00$1,250.00

Summary

  • Expression: HEK293
  • Binding assay: Yes (SPR)
  • Amino Acid Range: Ala27-Asp239
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q38J85

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% 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 38-45 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Cynomolgus IL-2 R beta/CD122 Protein 4627

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
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). {ECO:0000250|UniProtKB:P14784}.
Subellular location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14784}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P14784}.
Structure
SUBUNIT: 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). {ECO:0000250|UniProtKB:P14784}.
Domain
DOMAIN: Th
Target Relevance information above includes information from UniProt accession : Q38J85
The UniProt Consortium

Data

SPR with Cynomolgus IL-2 R beta/CD122 Protein
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).
HPLC of Cynomolgus IL-2 R beta/CD122 Protein
The purity of Cynomolgus IL-2 R beta is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Cynomolgus IL-2 R beta/CD122 Protein
Cynomolgus IL-2 R beta on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

Publications

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.




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