Recombinant Human IL-6 Protein Best Seller

R&D Systems, part of Bio-Techne | Catalog # 206-IL

R&D Systems, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
Carrier Free
206-IL-001MG/CF
206-IL-025/CF
Show More Sizes
206-IL-050/CF
206-IL-200/CF
Show Fewer Sizes
Catalog #
Availability
Size / Price
Qty
With Carrier
206-IL-200
206-IL-050
Show More Sizes
206-IL-01M
206-IL-010
Show Fewer Sizes
Print Quote
Bulk Order
100% Guarantee

Key Product Details

Source

E. coli

Accession #

P05231.1

Conjugate

Unconjugated

Applications

Bioactivity

View all IL-6 Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human IL-6 protein
Pro29-Met212

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.

N-terminal Sequence Analysis

Pro29

Predicted Molecular Mass

20.9 kDa

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.

Reviewed Applications

Read 26 reviews rated 4.7 using 206-IL in the following applications:

Scientific Data Images for Recombinant Human IL-6 Protein

Recombinant Human IL‑6 Protein SEC-MALS.

Recombinant Human IL-6 (Catalog # 206-IL) has a molecular weight (MW) of 23.1 kDa as analyzed by SEC-MALS, suggesting that this protein is a monomer.  MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).
Recombinant Human IL-6 Protein Bioactivity

Recombinant Human IL-6 Protein Bioactivity

Recombinant Human IL-6 (Catalog # 206-IL) stimulates cell proliferation of the T1165.85.2.1 mouse plasmacytoma cell line. The ED50 for this effect is 0.2-0.8 ng/mL.
Recombinant Human IL-6 Protein SDS-PAGE

Recombinant Human IL-6 Protein SDS-PAGE

1 μg/lane of Recombinant Human IL-6 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 21 kDa.
View 1 more images

Formulation, Preparation and Storage

Carrier Free
What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Carrier: 206-IL
Formulation Lyophilized from a 0.2 μm filtered solution in PBS and NaCl with BSA as a carrier protein.
Reconstitution Reconstitute at 100-200 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
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.
  • 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.
Carrier Free: 206-IL/CF
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.
  • 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.

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

Alternate Names

BSF-2, BSF2, IFNB2, IL6, MGI-2A

Entrez Gene IDs

3569 (Human); 16193 (Mouse); 24498 (Rat); 399500 (Porcine); 280826 (Bovine); 403985 (Canine); 102138971 (Cynomolgus Monkey); 100034196 (Equine); 493687 (Feline); 463288 (Primate); 100008733 (Rabbit)

Gene Symbol

IL6

UniProt

P05231.1

Additional IL-6 Products

Product Documents for Recombinant Human IL-6 Protein

Product Datasheets

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Download SDS 206-IL (with carrier)
Download SDS 206-IL/CF (carrier free)

Product Specific Notices for Recombinant Human IL-6 Protein

For research use only

Privacy and Cookie Policy
Site Map
© Copyright 2024 Bio-Techne. All Rights Reserved.