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Recombinant Human IL-12 R beta 2 Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 1959-B2B

R&D Systems, part of Bio-Techne
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1959-B2B-050

Key Product Details

Source

NS0

Accession #

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human IL-12 R beta 2 protein
Human IL-12 R beta2
(Lys24-Asn622)
Accession # Q99665-1
IEGRMD Human IgG1
(Pro100-Lys330)
6-His tag
N-terminus C-terminus

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Lys24

Predicted Molecular Mass

95 kDa

SDS-PAGE

112-133 kDa, reducing conditions

Activity

Measured by its binding ability in a functional ELISA.
When Recombinant Human IL‑12 (Catalog # 219-IL) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Recombinant Human IL‑12 R beta2 Fc that produces 50% of the optimal binding response is 0.015-0.09 μg/mL.

Scientific Data Images for Recombinant Human IL-12 R beta 2 Fc Chimera Protein, CF

Recombinant Human IL-12 R beta 2 Fc Chimera Protein Binding Activity

Recombinant Human IL-12 R beta 2 Fc Chimera Protein Binding Activity

When Recombinant Human IL-12 (Catalog # 219-IL) is immobilized at 0.5 µg/mL, Recombinant Human IL-12 R beta 2 Fc Chimera (Catalog # 1959-B2B) binds with an ED50 of 0.015-0.09 µg/mL.
Recombinant Human IL-12 R beta 2 Fc Chimera Protein SDS-PAGE

Recombinant Human IL-12 R beta 2 Fc Chimera Protein SDS-PAGE

1 μg/lane of Recombinant Human IL‑12 R beta2 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silverstaining, showing bands at 112-133 kDa and 220-260 kDa, respectively.

Formulation, Preparation and Storage

1959-B2B
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 250 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: IL-12 R beta 2

The high-affinity IL-12 receptor complex includes the 100-kDa IL-12 Receptor beta1 (IL-12 R beta1) and the 130-kDa IL-12 Receptor beta2 (IL-12 R beta2) subunits, both type I transmembrane proteins within the cytokine receptor superfamily (1, 2). Its ligand, IL-12, is a disulfide-linked dimer of 35-kDa (IL-12 alpha p35) and 40-kDa (IL-12 beta p40) subunits. IL-12 R beta2 binds IL-12 alpha and signals through Jak2, while IL-12 R beta1 binds IL-12 beta and signals through Tyk2 (3). IL-12 R beta1 is also a subunit of the IL-23 receptor complex (3). The 862 amino acid (aa) human IL-12 R beta2 includes a 23 aa signal peptide, a 599 aa extracellular domain (ECD) with five fibronectin type III (Fn III) domains, 8 potential N-glycosylation sites, and a WSXWS motif, a 21 aa transmembrane domain and a 219 aa cytoplasmic region with a Box 1 motif and a tyrosine phosphorylation site that both mediate intracellular signaling (3). Human IL-12 R beta2 ECD shares 69%, 67%, 79%, 81% and 82% aa sequence identity with mouse, rat, canine, porcine and bovine IL-12 R beta2, respectively. Human and mouse IL-12 R beta2 do not bind cross-species IL-12 (2). A human alternatively spliced 659 aa form contains a shortened, altered cytoplasmic sequence (4). Unlike IL-12 R beta1, which is constitutive in T cells, NK cells and B cells, IL-12 R beta2 expression is more limited (2). IL-12 R beta2 is expressed following STAT1 activation by IFN-gamma, IL-27 and/or T cell receptor stimulation of naïve T cells, allowing IL-12 to promote Th1, but not Th2, differentiation (5-7). Among B cells, surface expression is limited to naïve germinal center and memory B cells, and myeloma cells (2). Deletion of mouse IL-12 R beta2 causes systemic overexpression of IL-6, accelerated maturation of thymocytes, deficient regulatory T cell maturation and function, and reduced splenic T cell apoptosis (2, 8-10). These mice are susceptible to autoimmune diseases such as experimental autoimmune encephalitis and spontaneous B cell malignancies (2, 8‑10). In humans, polymorphism of the IL-12 R beta2 gene is associated with systemic sclerosis (11).

References

  1. Presky, D.H. et al. (1996) Proc. Natl. Acad. Sci. USA 93:14002.
  2. Pistoia, V. et al. (2009) J. Clin. Oncol. 27:4809.
  3. Zou, J. et al. (1997) J. Biol. Chem. 272:6073.
  4. SwissProt accession # Q99665
  5. Rogge, L. et al. (1997) J. Exp. Med. 185:825.
  6. Becskei, A. and M.J. Grusby (2007) FEBS Lett. 581:5199.
  7. Szabo, S.J. et al. (1997) J. Exp. Med. 185:817.
  8. Zhao, Z. et al. (2008) J. Immunol. 181:3870.
  9. Gran, B. et al. (2010) Exp. Mol. Pathol. 89:126.
  10. Airoldi, I. et al. (2005) Blood 106:3846.
  11. Bossini-Castillo, L. et al. (2012) Hum. Mol. Genet. 21: 926

Long Name

Interleukin 12 Receptor beta 2

Alternate Names

IL-12Rb2, IL12R beta 2, IL12RB2

Entrez Gene IDs

3595 (Human); 16162 (Mouse)

Gene Symbol

IL12RB2

UniProt

Additional IL-12 R beta 2 Products

Product Documents for Recombinant Human IL-12 R beta 2 Fc Chimera Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human IL-12 R beta 2 Fc Chimera Protein, CF

For research use only

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