Recombinant Human IL-6/IL-6R alpha Protein Chimera Summary
Details of Functionality |
Measured by its ability to inhibit M1 mouse myeloid leukemia cell proliferation. The ED50 for this effect is 2.5-12.5 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human IL-6/IL-6R alpha Complex protein Human IL-6R alpha (Leu20-Asp358) Accession # P08887 | GGGSGGGSGGGS | Human IL-6 Val30-Met212 Accession # P05231 | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Leu20 (Human IL-6R alpha)
|
Protein/Peptide Type |
Recombinant Proteins |
Gene |
IL6 |
Purity |
>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 |
|
Theoretical MW |
59 kDa. 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 |
78-93 kDa, reducing conditions
|
Publications |
Read Publications using 8954-SR in the following applications:
|
|
Packaging, Storage & Formulations
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.
- 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 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-6/IL-6R alpha Protein Chimera
Background
Interleukin-6 (IL-6) is a pleiotropic, alpha -helical, 22-28 kDa phosphorylated and variably glycosylated cytokine that plays important roles in the acute phase reaction, inflammation, hematopoiesis, bone metabolism, and cancer progression (1-5). Mature human IL-6 is 183 amino acids (aa) in length and shares 39% aa sequence identity with mouse and rat IL-6 (6). Alternative splicing generates several isoforms with internal deletions, some of which exhibit antagonistic properties (7-10). IL-6 induces signaling through a cell surface heterodimeric receptor complex composed of a ligand binding subunit (IL-6 R alpha) and a signal transducing subunit (gp130). IL-6 binds to IL-6 R alpha , triggering IL-6 R alpha association with gp130 and gp130 dimerization (11). gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM (12). Soluble forms of IL-6 R alpha are generated by both alternative splicing and proteolytic cleavage (5). In a mechanism known as trans-signaling, complexes of soluble IL-6 and IL-6 R alpha elicit responses from gp130-expressing cells that lack cell surface IL-6 R alpha (5). Trans-signaling enables a wider range of cell types to respond to IL-6, as the expression of gp130 is ubiquitous, while that of IL-6 R alpha is predominantly restricted to hepatocytes, monocytes, and resting lymphocytes (2, 5). Soluble splice forms of gp130 block trans-signaling from IL-6/IL-6 R alpha but not from other cytokines that use gp130 as a co-receptor (5, 13). IL-6, along with TNF-alpha and IL-1, drives the acute inflammatory response and the transition from acute inflammation to either acquired immunity or chronic inflammatory disease (1-5). When dysregulated, it contributes to chronic inflammation in obesity, insulin resistance, inflammatory bowel disease, arthritis, sepsis, and atherosclerosis (1, 2, 5). IL-6 can also function as an anti-inflammatory molecule, as in skeletal muscle where it is secreted in response to exercise (2). In addition, it enhances hematopoietic stem cell proliferation and the differentiation of Th17 cells, memory B cells, and plasma cells (1, 14).
- Mansell, A. and B.J. Jenkins (2013) Cytokine Growth Factor Rev. 24:249.
- Schuett, H. et al. (2009) Thromb. Haemost. 102:215.
- Erta, M. et al. (2012) Int. J. Biol. Sci. 8:1254.
- Garbers, C. et al. (2012) Cytokine Growth Factor Rev. 23:85.
- Mihara, M. et al. (2012) Clin. Sci. (Lond.) 122:143.
- Hirano, T. et al. (1986) Nature 324:73.
- Kestler, D.P. et al. (1995) Blood 86:4559.
- Kestler, D.P. et al. (1999) Am. J. Hematol. 61:169.
- Bihl, M.P. et al. (2002) Am. J. Respir. Cell Mol. Biol. 27:48.
- Alberti, L. et al. (2005) Cancer Res. 65:2.
- Murakami, M. et al. (1993) Science 260:1808.
- Muller-Newen, G. (2003) Sci. STKE 2003:PE40.
- Mitsuyama, K. et al. (2006) Clin. Exp. Immunol. 143:125.
- Cerutti, A. et al. (1998) J. Immunol. 160:2145.
FAQs for IL-6/IL-6R alpha Complex (8954-SR) (0)
Additional IL-6/IL-6R alpha Complex Products
Blogs on IL-6/IL-6R alpha Complex