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Recombinant Human IL-10 Protein, CF

R&D Systems | Catalog # 1064-ILB

Analyzed by SEC-MALS.
R&D Systems
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Key Product Details

  • R&D Systems E. coli-derived Recombinant Human IL-10 Protein (1064-ILB)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

Structure / Form

Noncovalently-linked homodimer

Applications

Bioactivity
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Product Specifications

Source

E. coli-derived human IL-10 protein
Ser19-Asn178, with a N-terminal Met

Purity

>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

19 kDa

SDS-PAGE

18 kDa, under reducing conditions.

Activity

Measured in a cell proliferation assay using MC/9‑2 mouse mast cells. Thompson-Snipes, L. et al. (1991) J. Exp. Med. 173:507. The ED50 for this effect is 0.075-0.750 ng/mL.

Scientific Data Images for Recombinant Human IL-10 Protein, CF

Recombinant Human IL‑10 Protein SEC-MALS.

Recombinant human IL-10 (Catalog # 1064-ILB) has a molecular weight (MW) of 36.7 kDa as analyzed by SEC-MALS, suggesting that this protein is a homodimer.  MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).

Recombinant Human IL‑10 Protein Bioactivity.

Measured in a cell proliferation assay using MC/9‑2 mouse mast cells. The ED50 for this effect is 0.075-0.750 ng/mL.

Recombinant Human IL‑10 Protein SDS-PAGE.

2 μg/lane of Recombinant Human IL‑10 Protein (Catalog # 1064-ILB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 18.4 kDa.

Formulation, Preparation, and Storage

1064-ILB
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 100-500 μg/mL in 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: IL-10

Interleukin 10, also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL‑10 family of alpha ‑helical cytokines that also includes IL‑19, IL‑20, IL‑22, IL‑24, and IL‑26/AK155 (1, 2). IL‑10 is secreted by many activated hematopoietic cell types as well as hepatic stellate cells, keratinocytes, and placental cytotrophoblasts (2-5). Mature human IL‑10 shares 72%-86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL‑10. Whereas human IL‑10 is active on mouse cells, mouse IL‑10 does not act on human cells (6, 7). IL‑10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer (6, 8, 9). The IL‑10 dimer binds to two IL‑10 R alpha /IL‑10 R1 chains, resulting in recruitment of two IL‑10 R beta /IL‑10 R2 chains and activation of a signaling cascade involving JAK1, TYK2, and STAT3 (10). IL‑10 R beta does not bind IL‑10 by itself but is required for signal transduction (1). IL‑10 R beta also associates with IL‑20 R alpha, IL‑22 R alpha, or IL‑28 R alpha to form the receptor complexes for IL‑22, IL‑26, IL‑28, and IL‑29 (11-13). IL‑10 is a critical molecule in the control of viral infections and allergic and autoimmune inflammation (14-16). It promotes phagocytic uptake and Th2 responses but suppresses antigen presentation and Th1 proinflammatory responses (2).

References

  1. Pestka, S. et al. (2004) Annu. Rev. Immunol. 22:929.
  2. Sabat, R. et al. (2010) Cytokine Growth Factor Rev. 21:331.
  3. Mathurin, P. et al. (2002) Am. J. Physiol. Gastrointest. Liver Physiol. 282:G981.
  4. Grewe, M. et al. (1995) J. Invest. Dermatol. 104:3.
  5. Szony, B.J. et al. (1999) Mol. Hum. Reprod. 5:1059.
  6. Vieira, P. et al. (1991) Proc. Natl. Acad. Sci. 88:1172.
  7. Hsu, D.-H. et al. (1990) Science 250:830.
  8. Windsor, W.T. et al. (1993) Biochemistry 32:8807.
  9. Syto, R. et al. (1998) Biochemistry 37:16943.
  10. Kotenko, S.V. et al. (1997) EMBO J. 16:5894.
  11. Kotenko, S.V. et al. (2000) J. Biol. Chem. 276:2725.
  12. Hor, S. et al. (2004) J. Biol. Chem. 279:33343.
  13. Sheppard, P. et al. (2003) Nat. Immunol. 4:63.
  14. Fitzgerald, D.C. et al. (2007) Nat. Immunol. 8:1372.
  15. Wu, K. et al. (2007) Cell. Mol. Immunol. 4:269.
  16. Blackburn, S.D. and E.J. Wherry (2007)Trends Microbiol. 15:143.

Long Name

Interleukin 10

Alternate Names

CSIF, GVHDS, IL10, IL10A, TGIF

Entrez Gene IDs

3586 (Human); 16153 (Mouse); 25325 (Rat); 397106 (Porcine); 403628 (Canine); 102133450 (Cynomolgus Monkey); 100034187 (Equine); 493683 (Feline); 100715618 (Guinea Pig); 2949786 (Viral)

Gene Symbol

IL10

UniProt

Additional IL-10 Products

Product Documents for Recombinant Human IL-10 Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human IL-10 Protein, CF

For research use only

Citations for Recombinant Human IL-10 Protein, CF

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