Detects human IL-13 R alpha 1 in ELISAs and Western blots. In sandwich ELISAs, less than 1% cross-reactivity with recombinant human (rh) IL‑13 R alpha 2, recombinant mouse (rm) IL-13 R alpha, rhIL-4 R, rhIL-5 R alpha, and rhIL-9 R is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human IL‑13 R alpha 1 Ala27-Thr343 (Thr130Ile) Accession # Q5JSL4
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Recombinant Human IL‑13 R alpha 1 Fc Chimera (Catalog # 146-IR)
Detection of IL‑13 R alpha 1 in Human Granulocytes by Flow Cytometry. Human peripheral blood granulocytes were stained with Human IL‑13 R alpha 1 Biotinylated Antigen Affinity‑purified Polyclonal Antibody (Catalog # BAF152, filled histogram) or control antibody (Catalog # BAF108, open histogram), followed by Streptavidin-Phycoerythrin (Catalog # F0040).
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
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.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-13 R alpha 1
Two type 1 membrane proteins belonging to the hemopoietin receptor family have been cloned and shown to bind IL-13 with differing affinities. The lower affinity IL-13 binding protein, previously designated IL-13 R alpha, IL-13 R alpha ' or NR4, is now referred to as IL-13 R alpha 1. The high-affinity IL-13 binding protein, previously also designated IL-13 R or IL-13 R alpha ', is now referred to as IL-13 R alpha 2.
The human IL-13 R alpha 1 was originally cloned based on sequence homology to the mouse IL-13 R alpha 1. The IL-13 R alpha 1 cDNA encodes a 427 amino acid (aa) residue precursor protein with a putative 21 aa residue signal peptide, a 324 aa residue extracellular domain, a 23 aa residue transmembrane region, and a 59 aa residue cytoplasmic tail. Human and mouse IL-13 R alpha 1 share 76% aa sequence identity. The extracellular domain of IL-13 R alpha 1 is also closely related to that of IL‑13 R alpha 2. IL‑13 R alpha 1 has been shown to combine with the IL-4 R alpha to form a high-affinity receptor complex capable of transducing an IL-13-dependent proliferative signal. The role of IL-13 R alpha 2 in IL-13 signaling remains to be elucidated.
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Donaldson, D.D. et al. (1998) J. Immunol. 161:2317.
Aman, M.J. et al. (1996) J. Biol. Chem. 271:29265.
Hilton, D.J. et al. (1996) Proc. Natl. Acad. Sci. USA 93:497.
Zhang, J.G. et al. (1997) J. Biol. Chem. 272:9474.
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The data collected includes not only links to publications in PubMed,
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