Detects human IL-13 R alpha 1 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant mouse IL-13 R alpha 1, recombinant human (rh) IL-13 R alpha 2, rhIL-4 R, rhIL-5 R beta, or rhIL-9 R is observed.
Monoclonal Mouse IgG2B Clone # 419718
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human IL‑13 R alpha 1 Ala27-Thr343 Accession # P78552
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of IL‑13 R alpha 1 in Human Blood Granulocytes by Flow Cytometry.
Human peripheral blood granulocytes were stained with (A) MouseAnti-Human Siglec-3/CD33 PE-conjugated Monoclonal Antibody (Catalog # FAB1137P) and (B) Mouse Anti-Human IL‑13 R alpha 1 Alexa Fluor® 700‑conjugated Monoclonal Antibody (Catalog # FAB1462N, filled histogram) or isotype control antibody (Catalog # IC0041N, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
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, 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) precursor protein with a putative 21 aa signal peptide, a 324 aa extracellular domain, a 23 aa transmembrane region and a 59 aa 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.
Caput, D. et al. (1996) J. Biol. Chem. 271:16921.
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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