Recombinant Human IL-13 R alpha 1 His-tag Protein, CF
Recombinant Human IL-13 R alpha 1 His-tag Protein, CF Summary
Product Specifications
Ala27-Thr343, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11424-IR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 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.
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Scientific Data
Recombinant Human IL‑13 R alpha 1 His-tag Protein (Catalog # 11424-IR) binds Recombinant Human IL-13 (213-ILB/CF) with an ED50 of 37.5-450 ng/mL.
2 μg/lane of Recombinant Human IL‑13 R alpha 1 His-tag Protein (Catalog # 11424-IR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 58-64 kDa, under reducing conditions.
Reconstitution Calculator
Background: IL-13 R alpha 1
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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