Recombinant Mouse Interleukin-2 Receptor Subunit Beta (IL2RB) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04689P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) l2rb.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) l2rb.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) l2rb.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) l2rb.

Recombinant Mouse Interleukin-2 Receptor Subunit Beta (IL2RB) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04689P
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Product Overview

Description Recombinant Mouse Interleukin-2 Receptor Subunit Beta (IL2RB) Protein (His) is produced by our E.coli expression system. This is a extracellular protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P16297
Target Symbol IL2RB
Synonyms Il2rbInterleukin-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
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence ASAAVKNCSHLECFYNSRANVSCMWSHEEALNVTTCHVHAKSNLRHWNKTCELTLVRQASWACNLILGSFPESQSLTSVDLLDINVVCWEEKGWRRVKTCDFHPFDNLRLVAPHSLQVLHIDTQRCNISWKVSQVSHYIEPYLEFEARRRLLGHSWEDASVLSLKQRQQWLFLEMLIPSTSYEVQVRVKAQRNNTGTWSPWSQPLTFRTRPADPMKE
Expression Range 24-240aa
Protein Length Extracellular Domain
Mol. Weight 29.0kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Cell surface.
Protein Families Type I cytokine receptor family, Type 4 subfamily
Database References

Gene Functions References

  1. The larger pool of IL-2Rbeta chains in CD8+ T cells is required to sustain IL-2 signaling and contributes to the quantitatively greater proliferative response to IL-2 relative to that of CD4+ mouse primary T cell cultures. PMID: 29259099
  2. Diabetes was accelerated in male and female NOD mice in which IL-2Rbeta signaling was modestly and selectively reduced in T cells. PMID: 29259102
  3. c-REL, but not IkappaBNS, controlled the generation of classical CD25(+)Foxp3(-) precursors via direct binding to the Cd25 locus; propose that CD4(+)GITR(+)CD122(+)CD25(-)Foxp3(-) cells represent a Treg pre-precursor population, whose transition into Treg precursors is mediated via c-REL PMID: 28652399
  4. Renal lesions are indeed modulated by intrinsic glomerular cells through the gamma-C/IL-2-beta receptor response, to date classically described only in immune cells. PMID: 28111009
  5. CBP physically associates with the IL-2 receptor beta-chain. CBP, found in the nucleus in resting CTLL-2 cells, relocates to the cytoplasm after IL-2 stimulation in an MEK/ERK pathway-dependent manner. Thus, IL-2-mediated acetylation plays an important role in the modulation of cytokine signaling and T cell fate. PMID: 27799311
  6. IL-2Rbeta-dependent signaling and CD103 functionally cooperate to maintain tolerance in the gut mucosa. PMID: 25527788
  7. Thymic development of CD4+Foxp3+ regulatory T cells (Tregs) is highly dysregulated in IL-2 receptor (2Rbeta)-deficient mice. PMID: 23315074
  8. CDCD11c+B220+CD122+ cells play an important role in xenograft rejection. Their absence in NOG mice may be critical in supporting the successful engraftment of xenotransplants. PMID: 23018460
  9. This study demonstrated that IL-12 signaling plays a complex role during the induction of tolerance as the presence of exogenous IL-12 and the lack of IL-12 signaling both prevent complete induction of tolerance. PMID: 22522341
  10. Continuous activation of the CD122/STAT-5 signaling pathway characterize regulatory lineage differentiation in the murine thymus. PMID: 21541329
  11. Knockout mice exhibited deficit in prepulse inhibition of acoustic startle reflex, significant reductions in acoustic startle reactivity, and modest differences in behavior in elevated plus-maze test. (IL-2/15 receptor-beta) PMID: 11864627
  12. role of the interleukin-2 receptor beta chain region between the two Stat5 docking sites in induction of interleukin-2 receptor alpha expression by interleukin-2 PMID: 12231477
  13. Depletion of IL-2 in vivo induces memory CD8+ T cell division by an IL-15-independent but by an IL-2/15 receptor beta-dependent mechanism, implying a novel process for antigen-independent homeostasis of memory CD8+ T cells in vivo. PMID: 15528339
  14. This study for the first time delineates the molecular mechanisms underlying regulation of mouse IL-2Rbeta gene transcription by Ets family proteins, partially with Egr-1, and thereby further elucidates the molecular basis of lymphocyte activation. PMID: 15752766
  15. The multivesicular regions were present in the cap structure of these granules, suggesting that the uNK cells of the Tg2Rbeta mice had cytotoxic activity. PMID: 16127247
  16. these cells make up a specialized subset of central memory T cells with distinguishable phenotypic characteristics, most notably the higher expression of CD122 and CD127 PMID: 16920913
  17. STAT5 binds to the promoter of the foxp3 gene suggesting that IL-2Rbeta-dependent STAT5 activation promotes Treg differentiation by regulating expression of foxp3. PMID: 17182565
  18. a signal mediated by IL-2Rbeta is essential for the development and homeostasis of Foxp3(+) Treg in vivo PMID: 17559173
  19. local blockade of the beta-chain of the IL-2R restored an immunosuppressive cytokine milieu in the lung that ameliorated both inflammation and airway hyperresponsiveness in experimental allergic asthma PMID: 18641329
  20. Common gamma-chain binding-dependent activation of the shared IL-15/IL-2 receptor beta/common gamma signaling pathway may play an important role in the activation of natural killer (NK) cells and CD8-positive T cells, resulting in tumor growth inhibition. PMID: 19050240
  21. IL-9Ralpha and IL-2Rbeta homodimers efficiently mediate constitutive activation of ALL-associated JAK1 mutants. PMID: 19139102
  22. subset of IL-2-dependent targets is indexed to a low IL-2R signaling threshold PMID: 19185518
  23. A population of memory CD8 T cells generated under sterile inflammatory conditions is identified by intermediate expression levels of CD122/CD44 and is involved in recall contact hypersensitivity reactions responsible for allergic contact dermatitis. PMID: 19265164
  24. IL2R beta-chain induces growth potential for glandular epithelial cells and an immune-privileged condition mediated by CD25+regulatory-T cells. PMID: 19293560

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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