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CD122 / IL-2RB  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: Human Cells  
10696-HCCH-5
10696-HCCH-20
10696-HCCH-10
5 µg 
20 µg 
10 µg 
/ 
/ 
/ 
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Description: Active  
Expression host: Human Cells  
10696-H02H-20
10696-H02H-10
20 µg 
10 µg 
/ 
/ 
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  • Slide 1
Expression host: Human Cells  
50792-M08H-5
50792-M08H-20
50792-M08H-10
5 µg 
20 µg 
10 µg 
/ 
/ 
/ 
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  • Slide 1
Expression host: Human Cells  
70082-D02H-5
70082-D02H-20
70082-D02H-10
5 µg 
20 µg 
10 µg 
/ 
/ 
/ 
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Expression host: Human Cells  
90328-C08H-50
90328-C08H-20
50 µg 
20 µg 
/ 
/ 
Add to Cart
  • Slide 1
Expression host: Human Cells  
90328-C02H-50
90328-C02H-20
50 µg 
20 µg 
/ 
/ 
Add to Cart
  • Slide 1

CD122 / IL-2RB Related Area

CD122 / IL-2RB Related Pathways

CD122 / IL-2RB Related Protein, Antibody, cDNA Gene, and ELISA Kits

CD122 / IL-2RB Summary & Protein Information

CD122 / IL-2RB Background

Gene Summary: The interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. The protein encoded by IL2RB gene represents the beta subunit and is a type I membrane protein. [provided by RefSeq, Jul 2008]
General information above from NCBI
Subunit 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. Interacts with HTLV-1 accessory protein p12I. {ECO:0000269|PubMed:12200137, ECO:0000269|PubMed:16293754, ECO:0000269|PubMed:16477002, ECO:0000269|PubMed:8648694}.
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.; The box 1 motif is required for JAK interaction and/or activation.
Subcellular location: Membrane; Single-pass type I membrane protein.
Sequence similarity: Belongs to the type I cytokine receptor family. Type 4 subfamily. {ECO:0000305}.; Contains 1 fibronectin type-III domain. {ECO:0000255|PROSITE-ProRule:PRU00316}.
General information above from UniProt

Interleukin-2 receptor (IL-2R) also known as High affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.

CD122 / IL-2RB Alternative Name

CD122 / IL-2RB Related Studies

  • Foss F. (2006) Clinical experience with denileukin diftitox (ONTAK). Semin Oncol. 33(1 Suppl 3): 11-6.
  • Sprent J, et al. (2001) T cell death and memory. Science. 293(5528): 245-8.
  • Teshigawara K, et al. (1987) Interleukin 2 high-affinity receptor expression requires two distinct binding proteins. J Exp Med. 165 (1): 223-38.
    • Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
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