Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to inhibit IL-13-dependent proliferation of TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.2-0.8 µg/mL in the presence of 4 ng/mL rmIL-13. |
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Source | Mouse myeloma cell line, NS0-derived mouse IL-13 R alpha 1 protein
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Accession # | |||||||||
N-terminal Sequence | Ala25 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Il13ra1 |
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Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 63 kDa (monomer). 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 | 100-120 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 200 μg/mL in sterile PBS. |
Mouse IL-13 receptor alpha one (IL‑13 R alpha 1), previously called NR4, IL-13 R alpha , and IL13R alpha ', is a member of the hemopoietin receptor family that was cloned on the basis of its conserved WSXWS motif. Mouse IL‑13 R alpha 1 encodes a 424 amino acid (aa) residue precursor type I membrane protein with a 26 aa residue signal peptide, a 314 aa residue extracellular domain (containing an immunoglobulin-like domain and a typical hemopoietin receptor domain), a 24 aa residue transmembrane region and a 60 aa residue cytoplasmic tail. Human IL‑13 R alpha 1, with 76% amino acid sequence identity to mouse IL‑13 R alpha 1, has also been cloned. In addition, a second human IL‑13 binding protein, designated IL‑13 R alpha 2 and previously known as IL‑13 R beta , IL‑13 R and IL‑13 R alpha , has been cloned from the Caki‑1 human renal carcinoma cell line. Murine IL‑13 R alpha 2 has been cloned from a mouse thymus cDNA library. The amino terminal 27 amino acid residues of the human and mouse IL‑13 R alpha 2 is nearly identical to that of a soluble mouse IL ‑3 binding proteinpurified from mouse serum and urine.
Both human and mouse IL‑13 R alpha 2 and mouse IL‑13 binding protein bind IL‑13 with high‑affinity. In cells transfected with mouse IL‑13 R alpha 1 only, low‑affinity binding with mouse IL13 is observed. However, in cells expressing both the mouse IL‑13 R alpha 1 and mouse IL4 receptor, a high affinity IL‑13 receptor complex capable of transducing an IL‑13 or IL‑4‑dependent proliferative signal, is generated.These results suggest that mouse IL‑13 R alpha 1, in addition to its role as a IL‑13 binding subunit in the IL‑13 receptor complex, can serve as an alternative to the common gamma chain for IL‑4 signaling.
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