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

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When Recombinant Human IL-12 Protein (Catalog# 219-IL) is immobilized at 1.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human IL‑12R beta 2 Fc Chimera Avi-tag (Catalog #  AVI10930) that ...read more
1 μg/lane of Biotinylated Recombinant Human IL‑12 R beta 2 Fc Chimera Avi-tag Protein (Catalog # AVI10930) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized bysilver ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Human IL-12 R beta 2 Fc Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-12 Protein (Catalog # 219-IL) is immobilized at 1.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human IL‑12 R beta 2 Fc Chimera Avi-tag (Catalog#  AVI10930) that produces 50% of the optimal binding response is 0.15‑1.50 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-12 R beta 2 protein
Human IL-12 RB2
(Cys28-Asn622)
Accession # Q99665.1
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Cys28
Structure / Form
Disulfide-linked homodimer
Biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
96 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
115-130 kDa, under reducing conditions.

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-12 R beta 2 Fc Avi-tag Protein, CF

  • IL-12 R beta 2
  • IL-12 receptor beta 2
  • IL-12 receptor subunit beta-2
  • IL12R beta 2
  • IL-12R subunit beta-2
  • IL12RB2
  • IL-12Rb2
  • IL-12R-beta-2
  • interleukin 12 receptor, beta 2
  • interleukin-12 receptor beta-2 chain
  • interleukin-12 receptor subunit beta-2

Background

IL-12 Receptor beta 2 (IL-12 R beta 2) is a member of the cytokine receptor superfamily and when combined with the highly homologous IL-12 R beta 1, forms the heterodimeric high affinity IL-12 receptor complex. Both receptors are type I transmembrane glycoproteins with homology to gp130, the common receptor beta -chain of the IL-6-like cytokine superfamily (ref). Mature human IL-12 R beta 2 consists of an extracellular domain (ECD) with five fibronectin type III (FnIII) domains and a WSXWS motif, a single transmembrane domain and a cytoplasmic region with a Box 1 motif and a tyrosine phosphorylation site that both mediate intracellular signaling (1). The ECD of human IL-12 R beta 2 shares 69% and 67% amino acid sequence identity with mouse and rat IL-12 R beta 2, respectively. Human and mouse IL-12 R beta 2 do not bind cross-species IL-12 (2). Alternative splicing creates a IL-12 R beta 2 with a shortened and altered cytoplasmic sequence (3). IL-12 R beta 1 and IL-12 R beta 2 are receptors for the IL-12 family, which includes IL-12, IL-23, IL-27 and IL-35 and they activate the Janus kinase (JAK)–STAT (signal transducer and activator of transcription) pathway of signal transduction (4). The receptor chains are utilized by the cytokines in different combinations, with IL-12RB2 binding to IL-12 and IL-35 (5). Unlike IL-12RB1, which is constitutive in T cells, NK cells and B cells, IL-12 R beta 2 expression is more limited (2). IL-12 R beta 2 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 (6-8). 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 beta 2 causes systemic overexpression of IL-6, accelerated maturation of thymocytes, deficient regulatory T cell maturation and function, and reduced splenic T cell apoptosis (2, 9-11). These mice are susceptible to autoimmune diseases such as experimental autoimmune encephalitis and spontaneous B cell malignancies (2, 9-11). In humans, polymorphism of the IL-12 R beta 2 gene is associated with systemic sclerosis (12). Our Avi-tag Biotinylated IL-12 R beta 2 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
  1. Zou, J. et al. (1997) J. Biol. Chem. 272:6073.
  2. Pistoia, V. et al. (2009) J. Clin. Oncol. 27:4809.
  3. Poltorak, A. et al. (2001) J Immunol 167:2106.
  4. Vignali, D.A. and Kuchroo, V.K. (2012) Immunol. 13:722.
  5. Jones, L.L. and Vignali, D.A. (2011) Immunol Res. 51:5.
  6. Rogge, L. et al. (1997) J. Exp. Med. 185:825.
  7. Becskei, A. and M.J. Grusby (2007) FEBS Lett. 581:5199.
  8. Szabo, S.J. et al. (1997) J. Exp. Med. 185:817.
  9. Zhao, Z. et al. (2008) J. Immunol. 181:3870.
  10. Gran, B. et al. (2010) Exp. Mol. Pathol. 89:126.
  11. Airoldi, I. et al. (2005) Blood 106:3846.
  12. Bossini-Castillo, L. et al. (2012) Hum. Mol. Genet. 21:926.

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