Measured by its binding ability in a full range functional ELISA. Recombinant Mouse IL-6 Protein (406-ML) is immobilized at 2.00 μg/mL (100 μL/well). Catalog # 1830-SR Recombinant Mouse IL-6R alpha (aa 20-357) ...read more
Recombinant Mouse IL-6R alpha (aa 20-357) Protein Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse IL-6 Protein (Catalog #
406-ML) is immobilized at 2.00 μg/mL, 100 μL/well, Recombinant Mouse IL-6R alpha Protein (Catalog # 1830-SR) binds with an ED50 of 30.0-300 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse IL-6R alpha protein Leu20-Glu357, with a C-terminal 10-His tag
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
39 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
60-66 kDa, reducing conditions
Publications
Read Publications using 1830-SR 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 with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse IL-6R alpha (aa 20-357) Protein
CD126
gp80
IL-6 R alpha
IL6Q
IL6R alpha
IL-6R alpha
IL6R
IL-6R-1
IL6RA
IL-6Ra
IL6RQ
interleukin 6 receptor
Background
Interleukin 6 (IL-6) is a multifunctional cytokine that exerts its activities by binding to a high-affinity receptor complex consisting of two membrane glycoproteins: an 80 kDa ligand binding subunit (IL-6 R alpha /CD126) and a 130 kDa nonligand-binding signal-transducing subunit (gp130/CD130) (1-4). The mouse IL-6 R alpha cDNA encodes a precursor type I transmembrane protein of 460 amino acids (aa) that contains a 19 aa signal sequence, a 345 aa extracellular ligand binding domain, a 21 aa transmembrane region, and a 75 aa cytoplasmic segment (2). The extracellular segment contains an Ig-like and a fibronectin-type III domain, plus a membrane proximal WSXWS motif. In their extracellular regions, mouse IL-6 R alpha shares 89%, 51% and 50% aa identity with rat, human and porcine IL-6 R alpha , respectively. Unlike gp130 that is expressed ubiquitously, the cellular distribution of IL-6 R alpha is predominantly limited to hepatocytes and leukocyte subpopulations such as monocytes, neutrophils, T and B cells. Soluble IL-6R alpha has been found in various body fluids (5). Two soluble receptor isoforms that arise either from proteolytic cleavage of the membrane-bound IL-6R alpha , or by alternative mRNA splicing (reported only in human) have been described (6, 7). Soluble IL-6 R alpha binds IL-6 with an affinity similar to that of the membrane-bound IL-6 R alpha . More importantly, the soluble IL-6 R alpha /IL-6 complex is capable of interacting with the membrane-bound gp130 to activate cells that lack an integral membrane IL-6 R alpha . It has been documented that elevated soluble IL-6 R is associated with numerous diseases including arthritic lesions, multiple myeloma and Crohn’s disease (6, 7).
Yamasaki, K. et al. (1988) Science 241:825.
Sugita, T. et al. (1990) J. Exp. Med. 171:2001.
Hibi, M. et al. (1990) Cell 63:1149.
Saito, M. et al. (1992) J. Immunol. 148:4066.
Novick, D. et al. (1989) J. Exp. Med. 170:1409.
Jones, S.A. et al. (2001) FASEB J. 15:43.
Jones, S.A. and S. Rose-John (2002) Biochim. Biophys. Acta 1592:251.
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