Recombinant Human IL-13 R alpha 1 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhIL-13 R alpha 1/Fc Chimera at 4 µg/mL (100 µL/well) can bind rhIL-13 with a linear range of 1‑100 ng/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human IL-13 R alpha 1 protein
Human IL-13 R alpha 1 Ala27 - Thr343 (Thr130Ile) Accession # Q5JSL4
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
64 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
110 kDa, reducing conditions
Publications
Read Publications using 146-IR in the following applications:
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.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-13 R alpha 1 Fc Chimera Protein, CF
bB128O4.2.1 (interleukin 13 receptor, alpha 1)
Cancer/testis antigen 19
CD213a1 antigen
CD213a1
CT19
IL-13 R alpha 1
IL13 receptor alpha-1 chain
IL-13 receptor subunit alpha-1
IL13R alpha 1
IL-13R subunit alpha-1
IL13R
IL13RA
IL-13Ra
IL13RA1
IL-13Ra1
IL-13R-alpha-1
interleukin 13 receptor, alpha 1
interleukin-13 receptor subunit alpha-1
NR4
Background
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 mouseIL-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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