Recombinant Human IL-6 GMP Protein, CF

Animal-Free.
  
  • Purity
    >97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a cell proliferation assay using T1165.85.2.1 mouse plasmacytoma cells. Nordan, R.P. et al. (1987) J. Immunol. 139:813. The ED50 for this effect is 0.2‑0.8 ng/mL.
    The specific activity of Recombinant Human IL-6 is approximately 1.1 x 105 IU/μg, which is calibrated against human IL‑6 WHO International Standard (NIBSC code: 89/548).
  • Source
    E. coli-derived Pro29-Met212 Produced using non-animal reagents in an animal-free laboratory.
    Manufactured and tested under cGMP guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis
    Pro29-Val-Pro-Pro-Gly-Glu-Asp-Ser-Lys-Asp
  • Predicted Molecular Mass
    20.9 kDa
  • SDS-PAGE
    20-21 kDa, reducing conditions
206-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS and NaCl.
Reconstitution Reconstitute at 100-200 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Data Images
GMP-grade Recombinant Human IL‑6 (Catalog # 206‑GMP) stimulates proliferation of T1165.85.2.1 mouse plasma­cytoma cell line. The ED50 for this effect is 0.2‑0.8 ng/mL.
1 μg/lane of GMP-grade Recombinant Human IL-6 (Catalog # 206-GMP) was resolved with SDS-PAGE under reducing conditions (R) and visualized by silver staining, showing a single band at 21 kDa. 
Mass Spectrometry
MALDI-TOF analysis of GMP-grade Recombinant Human IL-6 (Catalog #
206‑GMP). The major peak corresponds to the calculated molecular mass, 20910 Da. The minor peak at 21127 Da is a matrix-associated artifact of the MALDI-TOF.
Background: IL-6
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).
  • References:
    1. Mansell, A. and B.J. Jenkins (2013) Cytokine Growth Factor Rev. 24:249.
    2. Schuett, H. et al. (2009) Thromb. Haemost. 102:215.
    3. Erta, M. et al. (2012) Int. J. Biol. Sci. 8:1254.
    4. Garbers, C. et al. (2012) Cytokine Growth Factor Rev. 23:85.
    5. Mihara, M. et al. (2012) Clin. Sci. (Lond.) 122:143.
    6. Hirano, T. et al. (1986) Nature 324:73.
    7. Kestler, D.P. et al. (1995) Blood 86:4559.
    8. Kestler, D.P. et al. (1999) Am. J. Hematol. 61:169.
    9. Bihl, M.P. et al. (2002) Am. J. Respir. Cell Mol. Biol. 27:48.
    10. Alberti, L. et al. (2005) Cancer Res. 65:2.
    11. Murakami, M. et al. (1993) Science 260:1808.
    12. Muller-Newen, G. (2003) Sci. STKE 2003:PE40.
    13. Mitsuyama, K. et al. (2006) Clin. Exp. Immunol. 143:125.
    14. Cerutti, A. et al. (1998) J. Immunol. 160:2145.
  • Long Name:
    Interleukin 6
  • Entrez Gene IDs:
    3569 (Human); 16193 (Mouse); 24498 (Rat); 399500 (Porcine); 280826 (Bovine); 403985 (Canine); 100034196 (Equine); 493687 (Feline); 100008733 (Rabbit)
  • Alternate Names:
    B cell stimulatory factor-2; B-cell differentiation factor; BSF-2; BSF2CTL differentiation factor; CDF; HGFHSFIFNB2Hybridoma growth factor; IFN-beta-2; IL6; IL-6; IL-6B-cell stimulatory factor 2; Interferon beta-2; interleukin 6 (interferon, beta 2); interleukin BSF-2; interleukin-6; MGI-2A

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