Recombinant Human IL-13 R alpha 2 His-tag, CF Summary
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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.
11562-IR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 200 μg/mL in PBS. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Scientific Data
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Recombinant Human IL-13 R alpha 2 His-tag Protein (Catalog # 11562-IR) inhibits Recombinant Human IL-13 (213-ILB) induced proliferation in the TF-1 human erythroleukemic cells. The ED50 for this effect is 4.00-60.0 ng/mL.
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2 μg/lane of Recombinant Human IL-13 R alpha 2 His-tag Protein (Catalog # 11562-IR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 53-58 kDa, under reducing conditions.
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Background: IL-13 R alpha 2
Interleukin‑13 Receptor alpha 2 (IL‑13 R alpha 2), also known as IL‑13 binding protein, and CD213a2, is a widely expressed 55 kDa cytokine receptor that plays an important role in the Th2‑polarized immune responses characteristic of a variety of pathologies, including parasitic infections and allergic asthma (1, 2). Mature human IL‑13 R alpha 2 consists of a 317 amino acid (aa) extracellular domain with three fibronectin type‑III domains, a WSxWS motif, a 20 aa transmembrane segment, and a 17 aa cytoplasmic domain (3). Within the ECD, human IL‑13 R alpha 2 shares 64% and 62% aa sequence identity with mouse and rat IL‑13 R alpha 2, respectively. In both mouse and human, a 40 kDa‑50 kDa soluble form of IL‑13 R alpha 2 can be generated by MMP‑8 mediated shedding in vitro (4). Although this is assumed to occur in vivo in mouse, there is no evidence that shedding occurs in human (5‑7). In mouse, alternative splicing also leads to sIL‑13 R alpha 2, but again, this phenomenon apparently does not occur in human (6‑7). Thus, the biological effects of human IL‑13 R alpha 2 would appear to be mediated exclusively by membrane IL‑13 R alpha 2 (7). The biological effects of IL‑13 and IL‑4 are closely related in part due to a shared receptor system. IL‑13 binds to IL‑13 R alpha 1 which then forms a signaling complex with IL‑4 R alpha (8, 9). IL‑13 R alpha 2 functions as a decoy receptor by binding and internalizing IL‑13 and preventing it from signaling through the IL‑13 R alpha 1/IL‑4 R alpha complex (3, 10). IL‑13 R alpha 2 can also block IL‑4 induced responses by inhibiting IL‑4 bound IL‑13 R alpha 1/IL‑4 R alpha receptor complexes even though it does not itself bind IL‑4 (11, 12). Aside from its decoy function, IL‑13‑activated IL‑13 R alpha 2 directly promotes the development of tissue fibrosis by inducing the transcription of TGF‑ beta (13). Presumably, any human soluble IL‑13 R alpha 2, if it exists, will retain its ligand binding capability and attenuate responses to IL‑13 but not to IL‑4 (11, 14). The up‑regulation of transmembrane during Th2‑biased immune responses limits the extent of those responses (15‑17).
- Wynn, T.A. (2003) Annu. Rev. Immunol. 21:425.
- Tabata, Y. et al. (2007) Curr. Allergy Asthma Rep. 7:338.
- Caput, D. et al. (1996) J. Biol. Chem. 271:16921.
- Chen, W. et al. (2008) J. Allergy Clin. Immunol. 122:625.
- O’Toole, M. et al. (2008) Clin. Exp. Allergy 38:594.
- Chen, W. et al. (2009) J. Immunol. 183:7870.
- Kasaian, M.T. et al. (2011) J. Immunol. 187:561.
- Andrews, A.-L. et al. (2006) J. Immunol. 176:7456.
- Zurawski, S.M. et al. (1995) J. Biol. Chem. 270:13869.
- Donaldson, D.D. et al. (1998) J. Immunol. 161:2317.
- Andrews, A.-L. et al. (2006) J. Allergy Clin. Immunol. 118:858.
- Rahaman, S.O. et al. (2002) Cancer Res. 62:1103.
- Fichtner-Feigl, S. et al. (2006) Nat. Med. 12:99.
- Zhang, J.G. et al. (1997) J. Biol. Chem. 272:9474.
- Chiaramonte, M.G. et al. (2003) J. Exp. Med. 197:687.
- Morimoto, M. et al. (2009) J. Immunol. 183:1934.
- Zheng, T. et al. (2008) J. Immunol. 180:522.
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