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Recombinant Human IL-13 R alpha 1 Fc Avi-tag Protein, CF

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When Biotinylated Recombinant Human IL-13 R alpha 1 Fc Chimera Avi-tag (Catalog # AVI10436) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human IL-13 (213-ILB) binds with an ED50 of 10-80 ng/mL.
When Biotinylated Recombinant Human IL-13 R alpha 1 Fc Chimera Avi-tag (Catalog # AVI10436) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human IL-13 (213-ILB) binds with an ED50 of 10-80 ng/mL.
2 μg/lane of Biotinylated Recombinant Human IL-13 R alpha 1 Fc Chimera Avi-tag (AVI10436) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-13 R alpha 1 Fc Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human IL-13 R alpha 1 Fc Chimera Avi-tag (Catalog # AVI10436) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human IL-13 (Catalog # 213-ILB) binds with an ED50 of 10-80 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-13 R alpha 1 protein
Human IL-13 R alpha 1
(Ala27-Thr343)
Accession # AAB37127.1		IEGRMDHuman IgG1
(Pro100-Lys330)		Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Ala27
Structure / Form
Biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
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
65 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
93-103 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

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

Alternate Names for Recombinant Human IL-13 R alpha 1 Fc Avi-tag Protein, CF

  • bB128O4.2.1 (interleukin 13 receptor, alpha 1)
  • Cancer/testis antigen 19
  • CD213a1 antigen
  • CD213a1
  • CT19
  • IL-13 R alpha 1
  • IL13 receptor alpha-1 chain
  • IL-13 receptor subunit alpha-1
  • IL13R alpha 1
  • IL-13R subunit alpha-1
  • IL13R
  • IL13RA
  • IL-13Ra
  • IL13RA1
  • IL-13Ra1
  • IL-13R-alpha-1
  • interleukin 13 receptor, alpha 1
  • interleukin-13 receptor subunit alpha-1
  • NR4

Background

IL-13 RA1, also known as IL-13R and IL-13 RA, is a type I transmembrane protein. Its cDNA encodes a 427 aa precursor protein, with 322 aa extracellular domain, 24 aa transmembrane domain and 60 aa intracellular domain. Within the extracellular domain, human IL-13 RA1 shares 75% and 74% homology with mouse and rat IL-13 RA1, respectively. IL-13 RA1 expresses ubiquitously in all tissues with the highest level in heart, liver, skeletal muscle and ovary (1). As a receptor, IL-13 RA1 can function alone or as a heterodimer with IL-4R. Although both IL-4 and IL-13 signal through IL-4R/IL-13 RA1 heterodimer, there are distinct differences. IL-4 binds IL-4R with high affinity then binds IL-13 RA1 with low affinity. In contrast, IL-13 binds IL-13 RA1 with decent affinity, then binds IL-4R with high affinity (2). In addition, the N-terminal Fibronectin type III domain (D1) of IL-13 RA1 is only required for the binding of IL-13 not IL-4 (3,4). After binding to IL-4 or IL-13, the Tyr residues in the cytoplasmic domain of IL-13 RA get phosphorylated and then activate signaling proteins including Jak1, Tyk1, Tyk2, IRS-1, and STAT6 (5, 6). Alternative splicing generates soluble iL-13 RA1 missing the transmembrane domain (7). It not only functions as a decoy receptor for IL-13, but also is able to reduce fasting blood glucose, mediated by IL-4 (8). Higher expression of IL-13 RA1 are found in several cancers, often associated with poor prognosis in patients (9-11). Our Avi-tag Biotinylated human IL-13 RA1 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. Aman M.J. et al. (1996) J. Biol. Chem. 271:29265.
  2. LaPorte S.L. et al. (2008) Cell 132:259.
  3. Arima K. et al. (2005) J. Biol. Chem. 280:24915.
  4. Ito T, et al. (2009) J. Biol. Chem. 284:24289.
  5. Umeshita-Suyama R. et al. (2000) Int. Immunol. 12:1499.
  6. Roy B, et al. (2002) J. Leukoc. Biol. 72:580.
  7. Osawa M, et al. (2000) Immunogenetics 51:974.
  8. Rachmin I, et al. (2017) Am. J. Physiol. Endocrinol. Metab. 313:E663.
  9. Park M.H. et al. (2017) Ann, Surg. Oncol. 24:3780.
  10. Cao H, et al. (2016) Oncotarget 7:61183.
  11. Suzuki A, et al. (2015) Cytokine 75:79.

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