ELISA Capture: Human IL-13 R alpha 2 Antibody (Catalog # MAB6141) ELISA Detection: Human IL-13 R alpha 2 Biotinylated Antibody (Catalog # BAF614) Standard: Recombinant Human IL-13 R alpha 2 Fc Chimera (Catalog # 614-INS)
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.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for IL-13 R alpha 2 Antibody [Biotin]
cancer/testis antigen 19
IL-13 R alpha 2
IL-13 receptor subunit alpha-2
IL13R alpha 2
IL-13R subunit alpha-2
interleukin 13 binding protein
interleukin 13 receptor alpha 2 chain
interleukin 13 receptor, alpha 2
interleukin-13 receptor subunit alpha-2
Two type1 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 l 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 l, is now referred to as IL-13 R alpha 2.
Human IL-13 R alpha 2 was originally cloned from the Caki-1 human renal carcinoma cell line. The IL-13 R alpha 2 cDNA encodes a 380 amino acid (aa) residue precursor protein with a putative 26 aa residue signal peptide, a 317 residue extracellular domain, a 20 aa residue transmembrane region and a 17 aa residue cytoplasmic tail. Human and mouse IL-13 R alpha 2 share 59% aa sequence identity. The extracellular domain of IL-13 R alpha 2 is also closely related to that of IL-13 R alpha 1. However, the 17 aa residue cytoplasmic domain of IL-13 R alpha 2 is much shorter than that of IL-13 R alpha 1, suggesting that the two receptors are functionally distinct. IL-13 R alpha 1 has been shown to combine with the IL-4 R 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. The amino-terminal 27 aa residues of the human and mouse IL-13 R alpha 2 are nearly identical to that of a soluble mouse IL-13 binding protein purified from mouse serum and urine.
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.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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