Measured by its ability to neutralize IL‑6 R alpha -mediated inhibition of proliferation in the M1 mouse myeloid leukemia cell line. The Neutralization Dose (ND50) is typically 0.2-0.4 µg/mL in the presence of 30 ng/mL Recombinant Human IL‑6 R alpha and 30 ng/mL Recombinant Human IL‑6.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
IL‑6 R alpha Enhancement of IL‑6‑dependent Inhibition of Cell Proliferation and Neutralization by Human IL‑6 R alpha Antibody.
Recombinant Human IL‑6 R alpha (Catalog # 227‑SR) enhances Recombinant Human IL‑6 (Catalog # 206‑IL) inhibition of proliferation in the M1 mouse myeloid leukemia cell line in a dose-dependent manner (orange line). Enhancement of Recombinant Human IL‑6 (30 ng/mL) activity elicited by Recombinant Human IL‑6 R alpha (30 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IL‑6 R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF‑227‑NA). The ND50 is typically 0.2‑0.4 µg/mL.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
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.
Background: IL-6 R alpha
The multifunctional factor interleukin 6 (IL-6) exerts its activities through binding to a high-affinity receptor complex consisting of two membrane glycoproteins: an 80 kDa component receptor that binds IL-6 with low affinity (IL-6 R alpha ) and a signal-transducing component of 130 kDa (gp130) that does not bind IL-6 by itself, but is required for high-affinity binding of IL-6 by the complex. Both components of the receptor complex, IL-6 R alpha and gp130 have been cloned, sequenced, and expressed (1-4).
A soluble form of the IL-6 R alpha has been found in the urine of healthy adult humans (5). This soluble receptor apparently arises from proteolytic cleavage of membrane-bound IL-6 R alpha. No naturally-occurring mRNA encoding a truncated form of the IL-6 R alpha has been reported. Soluble forms of human and murine IL-6 R alpha s have been constructed, however, by insertion of termination codons into the regions of the IL-6 R alpha cDNAs encoding the external portions of the receptors and prior to the transmembrane domains. These soluble receptors have been expressed in COS-7 and CHO cells and have been shown to bind to IL-6 in solution and to augment the activity of IL-6 as a result of the binding of the IL-6/IL-6 R alpha complex to membrane-bound gp130 (6, 7).
Yamasaki et al. (1988) Science 241:825.
Baumann et al. (1990) J. Biol. Chem. 265:19853.
Hibi et al. (1990) Cell 63:1149.
Schooltink et al. (1991) Eur. J. Biochem. 277:659.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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