Recombinant Human IL-11 R alpha Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IL-11 R alpha Protein, CF Summary

Details of Functionality
Measured by its ability to bind recombinant human IL-11 in a functional ELISA with an estimated Kd <1 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-11 R alpha protein
Ser24-Val363, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser24 & Cys26
Protein/Peptide Type
Recombinant Proteins
Gene
IL11RA
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
38 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
40-55 kDa, reducing conditions
Publications
Read Publications using
8895-MR in the following applications:

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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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-11 R alpha Protein, CF

  • AI314697
  • GP130
  • IL-11 R alpha
  • IL11R alpha
  • IL11RA
  • IL-11Ra
  • Il11ra2
  • NR1

Background

Interleukin-11 receptor alpha (IL-11 R alpha ) is a 49 kDa type I transmembrane member of the gp130 subfamily of the hematopoietic cytokine receptor family (1-3). Mature human IL-11 R alpha consists of a 347 amino acid (aa) extracellular domain (ECD) that contains a C2 type Ig-like domain, two fibronectin type III domains, two potential glycosylation sites, and a WSxWS motif, followed by a 21 aa transmembrane region and a 31 aa cytoplasmic domain (4). Within the ECD, human IL-11 R alpha shares 84%, 82%, 90%, and 86% aa sequence identity with mouse, rat, equine, and bovine IL-11 R alpha , respectively. Alternative splicing generates an additional isoform that lacks the cytoplasmic domain (4). Upon low affinity binding to IL-11, IL-11 R alpha associates with gp130 to form a high affinity receptor complex (1, 3). gp130 also functions as a subunit in the receptors for Cardiotrophin-1, CNTF, IL-6, IL-27, IL-31, LIF, and Oncostatin M (5). IL-11 R alpha is widely expressed in adults, embryos, and embryonic stem cells (4, 6, 7). Deletion of IL-11 R alpha in female mice causes faulty decidualization, lack of decidual NK cells, and infertility (8-10). IL-11 is anti-apoptotic for oligodendrocytes, and lack of IL-11 R alpha increases the severity of experimental autoimmune encephalitis (11, 12). IL-11 R alpha is also anti-apoptotic for colonic epithelia, and increased IL-11 signaling may be a factor in inflammation-associated gastrointestinal cancer development (3, 13). IL-11 R alpha enhances osteoclast differentiation and bone remodeling but inhibits adipocyte differentiation (1, 2). Recombinant soluble IL-11 R alpha confers IL-11 responsiveness to cells expressing gp130, while in cells expressing transmembrane IL-11 R alpha and gp130, soluble IL-11 R alpha acts as an IL-11 antagonist (14-16).
  1. Sims, N.A. and N.C. Walsh (2010) BMB Reports 43:513.
  2. White, U.A. and J.M. Stephens (2011) Curr. Pharm. Des. 17:340.
  3. Kiessling, S. et al. (2004) J. Biol. Chem. 279:10304.
  4. Cherel, M. et al. (1995) Blood 86:2534.
  5. Garbers, C. et al. (2012) Cytokine Growth Factor Rev. 23:85.
  6. Hilton, D.J. et al. (1994) EMBO J. 13:4765.
  7. Davidson, A.J. et al. (1997) Stem Cells 15:119.
  8. Paiva, P. et al. (2009) Cytokine Growth Factor Rev. 20:319.
  9. Robb, L. et al. (1998) Nat. Med. 4:303.
  10. Ain, R. et al. (2004) Dev. Dyn. 231:700.
  11. Gurfein, B.T. et al. (2009) J. Immunol. 183:4229.
  12. Zhang, J. et al. (2011) J. Immunol. 187:1129.
  13. Putoczki, T. and M. Ernst (2010) J. Leukoc. Biol. 88:1109.
  14. Curtis, D.J. et al. (1997) Blood 90:4403.
  15. Baumann, H. et al. (1996) J. Immunol. 157:284.
  16. Karow, J. et al. (1996) Biochem. J. 318:489.

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Publications for IL-11R alpha (8895-MR)(4)

We have publications tested in 2 confirmed species: Human, Insect.

We have publications tested in 1 application: Bioassay.


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Bioassay
(4)
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(3)
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(1)
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Bioinformatics

Gene Symbol IL11RA
Uniprot