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.
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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