Recombinant Human IL-13 R alpha 1 His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant
Human IL-13 R alpha 1 His-tag (Catalog # 11424-IR) binds
Recombinant Human IL-13 (Catalog #
213-ILB/CF) with an ED 50 of 37.5‑450 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human IL-13 R alpha 1 protein Ala27-Thr343, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala27 |
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 |
|
Theoretical MW |
37 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 |
58-64 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 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-13 R alpha 1 His-tag Protein, CF
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).
- Aman M.J. et al. (1996) J. Biol. Chem. 271:29265.
- LaPorte S.L. et al. (2008) Cell 132:259.
- Arima K. et al. (2005) J. Biol. Chem. 280:24915.
- Ito T, et al. (2009) J. Biol. Chem. 284:24289.
- Umeshita-Suyama R. et al. (2000) Int. Immunol. 12:1499.
- Roy B, et al. (2002) J. Leukoc. Biol. 72:580.
- Osawa M, et al. (2000) Immunogenetics 51:974.
- Rachmin I, et al. (2017) Am. J. Physiol. Endocrinol. Metab. 313:E663.
- Park M.H. et al. (2017) Ann, Surg. Oncol. 24:3780.
- Cao H, et al. (2016) Oncotarget 7:61183.
- Suzuki A, et al. (2015) Cytokine 75:79.
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